Module 1 Flashcards

1
Q

Define cell

A

The simplest collection of matter that can be alive

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2
Q

How many species be classified into groups

A

Based on structure and DNA sequence

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3
Q

Highest level of classification

A

Domain: Bacteria, Archaea, Eukarya

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4
Q

Name the 4 Kingdoms

A

Plantae, Fungi, Animalia, Protist

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5
Q

Size of plant and animal cells

A

10-100µm in diameter

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6
Q

What is the size of a bacteria cell?

A

1-5 µm in diameter

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7
Q

Why are cells limited to a certain size?

A

SA proportional to diameter squared, but vol proportional to diameter cubed.
- thus a small cell has a greater SA:vol ratio

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8
Q

3 important parameters in microscopy

A

Magnification, resolution, contrast

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9
Q

Define magnification

A

Ratio of image size to real size

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10
Q

Define resolution

A

Clarity of the image

  • the minimum distance that can separate two points that still remain identifiable as separate points when viewed through a microscope.
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11
Q

Contrast

A

The difference between light and dark areas of the image

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12
Q

What can you do to contrast?

A

Enhance, by staining

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13
Q

Magnification of light microscopy

A

1000x

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14
Q

What limits greater magnification of light microscopy

A

Resolution

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15
Q

What is the limit for resolution for light microscopy

A

0.2µm

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16
Q

How is the power of light microscopy enhanced

A

Staining and imaging techniques

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17
Q

Advantage of light microscopy over SEM and TEM

A

Light microscopy allows samples to be living

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18
Q

Difference between EM and LM

A

EM focuses electrons rather than light on a specimen

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19
Q

What is the relationship between resolution and wavelength

A

Resolution is inversely proportional to wavelength

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20
Q

Why do electrons allow higher resolutions

A

Because of their shorter wavelengths

  • Shorter wavelengths of electrons increase resolution such that intracellular structures may be “seen”
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21
Q

How many times fold is the improvement of EM on LM

A

100x

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22
Q

What is the process of SEM

A

Scans the surface of the specimen which has been coated in a thin film of gold.

Electrons excite the gold atoms to generate a 3-D image of the surface of a specimen.

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23
Q

Something common between EM and SEM

A

Images are grayscale, but can be coloured artificially.

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24
Q

What is TEM used for

A

To examine the cell’s internal structure

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25
Q

What is the process of TEM

A

Electron beam passes through a thin section of a specimen that has been stained with heavy metals. The scattered electrons are focused by electromagnets to generate an image

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26
Q

What cells can SEM and TEM be used on

A

Processed dead cells.

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27
Q

Structures of animal cell (8)

A
  • nucleus
  • ER (rough and smooth)
  • cytoskeleton: microfilaments, intermediate filaments, microtubules
  • microvilli
  • mitochondrion
  • golgi
  • ribosome
  • plasma membrane
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28
Q

Structures of a plant cell (8)

A
  • nucleus
  • ER (rough and smooth)
  • mitochondrion
  • chloroplast
  • central vacuole
  • golgi
  • plasmodesmata
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29
Q

How did the complex structure of the eukaryotic cell evolve?(5)

A
  • mitochondria resemble bacteria
  • prokaryotic cells were engulfed by early eukaryotic cells
  • established a stable relationship of benefit to both parties
  • engulfed prokaryotes evolved into mitochondria
  • similar proposal for chloroplasts airing from photosynthetic prokaryotes.
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30
Q

Draw the endosymbiont theory diagram and label

A

.

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31
Q

Composition of a typical prokaryotic cell

A
Water 70%
Protein 15%
Nucleic acids 7%
Carbohydrates 3%
Lipids 2%
Other small molecules 1%
Inorganic ions 1%
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32
Q

Major atomic constituents of biological macromolecules

A

O>C>H>N

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33
Q

Building blocks -> higher order of structures

A

Aa - proteins
nucleobases - nucleic acids (RNA, DNA)
Simple carbohydrates - Complex carbohydrates
Lipids

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34
Q

Supramolecular assmeblies

A
  • membranes
  • ribosomes
  • chromatin
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35
Q

Organelles

A
  • nucleus
  • mitochondria
  • golgi
  • ER
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36
Q

Difference between carbon chain and rings

A
  • more stable and soluble than linear structures
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37
Q

4 macromolecules

A
  1. Polysaccharides (complex carbohydrates)
  2. Nucleic acids (DNA and RNA)
  3. proteins
  4. Lipids
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38
Q

4 levels of carbohydrates

A
  1. Monosaccharides
  2. Disaccharides
  3. Oligosaccharides
  4. Polysaccharides
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39
Q

Hexose monosaccharides

A

Building blocks of higher order carbohydrates

- 6 carbons

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40
Q

Pentose monosaccharides

A

Usually part of larger molecules eg nucleic acids

- 5 carbons

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41
Q

What are Disaccharides

A

Two monosaccharides joined together

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42
Q

What makes up sucrose

A

Glucose + fructose

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43
Q

What makes lactose

A

Galactose + glucose

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44
Q

What makes up Maltose

A

Glucose + glucose

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45
Q

What are oligosaccharides

A

3 to approx 10 linked monosaccharides

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46
Q

How long are polysaccharides

A

Approx >10 linked monosaccharides

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47
Q

What is amylose made of

A

Alpha glucose linearly linked

- forms spiral

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48
Q

What is amylopectin

A

Alpha glucose linked in chains, but with branches

- like amylose with branches

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49
Q

What bonds are between glucose monomers in amylose and amylopectin and glycogen

A

Alpha1,4 glycosidic bonds

Alpha1,6 glycosidic bonds at branch-points

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50
Q

Compare amylopectin to glycogen

A

Glycogen is more branched

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51
Q

What is cellulose made of

A

beta glucose linked with beta1,4 glycosidic bonds

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52
Q

What two forms can glucose be in

A

Linear and ring

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53
Q

Different between alpha and beta glucose

A

OH on C1 is below on Alpha

Above on Beta

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54
Q

2 forms of starch

A

Amylose and amylopectin

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55
Q

What does the glucose chain look like in cellulose

A

OH alternating between up and down

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56
Q

Functions of carbohydrates (3)

A
  1. Cell recognition
  2. Energy (energy storage as polysaccharide)
  3. Structure
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57
Q

Why can’t cellulose be used as an energy source

A

Can only break alpha1,4 bonds in our body. Can’t break Beta1,4 bonds = can’t digest

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58
Q

What is the structure of cellulose

A

Chains of beta glucose monomers linked by beta1,4 bonds.

H bonding between the glucose chains

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59
Q

3 characteristics of lipids

A
  • not polymers
  • heterogeneous
  • hydrophobic
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60
Q

4 types of lipids

A
  • triacylglycerol
  • steroids (sterols)
  • phospholipids
  • fat soluble vitamins
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61
Q

Functions of lipids (3)

A
  1. Structural
  2. Regulatory
  3. Energy
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62
Q

2 structural lipids

A

Cholesterol and phospholipids in the cell membrane

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63
Q

What type of lipid is cholesterol

A

A steroid

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64
Q

How do phospholipids differ from triacyglycerol

A

Phospholipids have 2 chains of fatty acids and a phosphate head. Triacyglycerol have 3.

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65
Q

3 Steroids

A

Cholesterol
Testosterone
Oestrogen

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66
Q

Why do lipids make much more energy than fat

A

more carbons

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67
Q

3 components of nucleic acid

A

phosphate, (de)oxyribose sugar, nitrogenous base

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68
Q

Difference between deoxyribose and oxyribose

A

OH on C2 in RNA, H on C2 in DNA

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69
Q

What are proteins

A

Molecules by which cells perform their functions in the whole organism

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70
Q

1 gene codes for 1 protein

A

.

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71
Q

one gene can code for many proteins

A

the proteins are slightly different.

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72
Q

Functions of proteins

A
  • structural
  • regulatory
  • contractile
  • transport
  • storage
  • protective
  • catalytic
  • toxic
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73
Q

Example of structural protein

A

Collagen - skin and bones

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74
Q

Eg of regulatory protein

A

Insulin - a peptide hormone

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75
Q

Eg of contractile protein

A

Actin, myosin - muscle proteins

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76
Q

eg of transport protein

A

Hb - carries O2 around body

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77
Q

Eg of storage protein

A

egg white (albumin), seed proteins

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78
Q

eg of protective protein

A

Antibodies - immune proteins

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79
Q

eg of catalytic protein

A

amylase, RNA polymerase - enzymes

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80
Q

eg of toxic protein

A

Botulinum toxin, diphtheria toxin.

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81
Q

Size of bacterial cell

A

1µm^3

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82
Q

Old view of prokaryotes

A
  • homogenous static structures
  • undifferentiated - no behaviour
  • sacs of jumbled enzymes/proteins
  • small size, lack of organelles
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83
Q

Limiting factors for bacteria reproduction

A
  • nutrients
  • competition
  • space
  • build up of toxins
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84
Q

New view of bacterial cell biology

A
  • highly ordered and dynamic
  • capable of polarising and differentiation into cell types
  • intracellular organisation - protein localisation, DNA and lipids
  • signal each other to coordinate multicellular actions (3 languages: gram pos to gram pos, gram neg to gram neg, universal)
  • exhibit learning behaviour - anticipate changes in their environment (Pavolonian conditioning)
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85
Q

Structures in Bacteria

A
  • fimbriae
  • nucleoid
  • ribosomes
  • plasma membrane
  • cell wall
  • capsule
  • flagella
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86
Q

Width of bacteria

A

0.5µm

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87
Q

What is the cell wall of bacteria made of

A

Peptidoglycan

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88
Q

Function of cell wall of bacteria

A
  1. Structure: Rigid macromolecular layer that provides strength to cell
  2. Protection: Protects cells from osmotic lysis and confers cell shape.
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89
Q

What do antibiotics target?

A

The cell wall.

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90
Q

Structure of bacterial cell wall

A

NAG NAM (carbohydrate backbone with peptide side chains) linked up by peptide cross bridge

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91
Q

Difference in structure between gram positive and gram neg cell wall

A

Gram positive bacteria have a thicker peptidoglycan layer (20-80nm). Gram neg bacteria have a thin layer of peptidoglycan (5-10nm).

Gram neg have a thin layer of peptidoglycan between inner and outer membranes

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92
Q

Thickness of Gram-positive bacterial cell wall

A

20-80nm

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93
Q

Test observations for gram-pos vs gram-neg

A

For gram pos, Peptidoglycan traps crystal violet, which masks the safranin dye.

  • so much peptidoglycan that can’t wash away with alc
  • when iodine enters, an iodine-crystal violet copmlex forms.
  • too large to pass through thick cell wall -> not removed by
  • no effect of safranin

For gram neg, crystal violet is easily rinsed away, revealing the red safranin dye.

  • thin layer of peptidoglycan -> take up crystal violet
  • washed away with ethanol
  • cells take up safranin
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94
Q

Thickness of gram neg cell wall

A

5-10nm

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95
Q

What constitutes the cell wall of gram neg bacteria

A

A thin peptidoglycan layer under an outer membrane

- outer membrane contains lipopolysaccharides

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96
Q

What is the outer membrane of gram-negative bacteria made of

A

Lipopolysaccharide (LPS)

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97
Q

colour of gram neg and gram pos

A

Gram pos = purple

Gram neg = red

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98
Q

Process of gram staining

A
  1. Application of crystal violet (purple dye)
  2. Application of iodine (mordant)
  3. alcohol wash (decolorisation)
  4. application of safranin (counterstain)
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99
Q

4 Unique structure found only in prokaryotes

A
  1. bacterial flagella
  2. Cell surface layers: capsules and slime layers
  3. Bacterial endospores
  4. Fimbriae
  5. peptidoglycan (only in prok)
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100
Q

Structure of flagella

A
  • MOTILE bacteria produce flagella
    = long flexible appendage resembling “tails”
  • made of protein
    10 - 20nm in diameter
    5 - 10/cell
  • number of flagella and location on cell surface varies
  • act like a propeller: cell rotates them to move through a liquid medium
  • attached to cytoplasmic membrane.
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101
Q

What allows bacteria to move in LIQUID MEDIUM

A

flagella

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102
Q

How wide are flagella

A

10-20nm

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103
Q

What are the 3 major sections of flagella

A
  1. Long filament
  2. Hook
  3. Basal body
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104
Q

Describe the long filament of flagella

A
  • extends into the surrounding medium.
  • rigid
  • 50kDA
  • 4.5µm in diameter
  • composed of subunits (flagellin) - 20000 per filament
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105
Q

What are the subunits of flagella filament

A

Flagellin

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106
Q

How wide are flagella

A

10-20nm in diameter

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107
Q

How many subunits are in flagella

A

20000

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108
Q

Describe the hook of the bacterial flagella

A
  • Curved section connecting the filament to the cell surface
  • flexible
  • motor. Drives rotation.
  • couples motor to filament
  • apply torque -> flagellum rotates
  • couples torque
  • couples rigid pendulum to motor
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109
Q

Describe the basal body of flagella

A

Anchors the flagella into the cell membrane of the bacterium by special disc-shaped structures called rings or plates
- bacteria can rotate flagellum into clockwise or counterclockwise direction

  • direction depends on what they do in liquid medium.
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110
Q

What are the special disc -shaped structures in basal body of flagella called

A

Rings or plates

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111
Q

Describe chemotaxis in bacteria

A

movement of bacteria along a concentration gradient towards a chemical attractant or away from a a chemical repellent

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112
Q

What is the default state of motor

A

CCW

= run

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113
Q

Peritrichous

A

having flagella (tail like projections) all over its surface.

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114
Q

What does CW rotation of flagella result in

A

Tumble - flagella of peritrichous bacterium are pushed apart

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115
Q

How are the flagella in peritrichous bacteria arranged in CCW rotation

A

bundled together = run

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116
Q

How fast can bacteria “run”

A

10 bodylengths/sec

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117
Q

Do bacterium operate in a coordinated bundle?

A

No

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118
Q

Nature of movement of bacteria

A

Random

- tumbles promote random rotational turns during swimming.

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119
Q

Describe the mechanism of chemotaxis

A

Bacteria sense the change in chemical conc outside the cell over TIME -> temporal gradients
- thus respond to the change in conc as the cell moves.

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120
Q

Why can’t bacteria sense spatial gradient?

A

Because they are too small

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121
Q

How do they sense the chemical concentration over time?

A

Arrays of chemoreceptors

- hexagonal arrangement.

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122
Q

How large are fimbriae?

A

2-8nm in diameter
1µm in length
100-1000/cell

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123
Q

Describe the structure of fimbriae

A

Adhesins = bind to SPECIFIC receptors on the surface of cells.

  • mediate attachment.
  • vary adhesion to exploit different environments

Fimbrins = protein subunits helically wound with pore down centre polymerise to form fibres.

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124
Q

What is adhesin on fimbriae?

A

Allows bind to specific receptors on the surface of cells. Mediate attachment.
- vary adhesin to exploit different environments

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125
Q

What are fimbrins?

A

protein subunits helically wound with pore down centre polymerise to form fibres in fimbriae.

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126
Q

What are capsules and slime layers made of?

A

Glycocalyx

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127
Q

What is glycocalyx?

A

A gelatinous polysaccharide and/or polypeptide outer covering
- forms a sticky meshwork of fibers

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128
Q

What is a capsule?

A

Glycocalyx organised into a defined structure attached firmly to cell wall

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129
Q

What is slime layer?

A

Glycocalyx disorganised without cell shape, attached loosely to cell wall.

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130
Q

What functions do capsules serve? (4)

A
  1. Virulence factors: protect bacteria from phagocytosis and engulfment by immune cells
    - slippery capsule makes it difficult for a phagocyte to establish contact with invading bacterium
  2. Adhere to cell surfaces -> colonisation
  3. Source of nutrients and energy to microbes
    - eg strep doc mutans colonise teeth: ferments suga in the capsule and acid byproducts contribute to tooth decay.
  4. prevent cell from drying out (desiccation)
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131
Q

How does the capsule protect bacteria from phagocytosis and engulfment by immune cells?

A

Slippery capsule makes it difficult for a phagocyte to establish contact with invading bacterium

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132
Q

Why is adherence to cell surfaces important for bacteria?

A

Important first step in colonisation and sometimes leads to disease.
- eg structures such as medical implants, catheters and so on

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133
Q

Example of capsules being a source of nutrient and energy to microbes

A

Streptococcus mutans = colonise teeth, ferments the sugar in the capsule and acid byproducts contribute to tooth decay.

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134
Q

What are bacterial endospores

A

highly differentiated cells resistant to heat, harsh chemicals, antibiotics/disinfectants and radiation: “dormant” stage of bacterial life cycle.

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135
Q

What type of bacteria can form endospores?

A

Some gram-positive: members of genus Bacillus and Clostridium

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136
Q

When do endospores form and germinate

A

Formed during unfavourable growth conditions

Germinate under favourable conditions.

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137
Q

What is the function of endospores

A

protect cell from stress. Wait for more favourable conditions to germinate

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138
Q

is bacterial endospores transmissible?

A

Highly transmissible

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139
Q

Types of bacterial endospores

A
  • Terminal spores
  • subterminal spores
  • central spores
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140
Q

Life cycle of an endospore- forming bacterium

A
  1. Vegetative cell
  2. Developing spore form on one end of cell (asymmetric cell division)
  3. Chromosome replication.
  4. Spore matures.
    • mature spore is very different from vegetative, but genetically identical. Highly differentiated.
      • mature spore is very resistant to temp, chemical etc
  5. vegetative cell dies.
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141
Q

Structure of Bacterial endospore

A
  • Exosporium
  • spore coat
  • core wall
  • cortex - has peptidoglycan- cell wall
  • DNA
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142
Q

4 important properties of spores

A
  1. Heat and radiation resistant
  2. Water content low (10-25%)
  3. High in Ca2+ and dipicolinic acid
  4. Low metabolic activity/dormant ( good for dispersal and protect genome).
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143
Q

What make the endospore heat resistant?

A
  1. Low water content

2. Dipicolinic acid.

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144
Q

Size of prokaryotic cells and eukaryotic cells

A
Pro = <5mm
Euka = >10mm
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145
Q

Difference between pork and euka cells

A
  1. No cytoskeleton in prokaryotes. Always have cytoskeleton in eukaryotic cells.
  2. Ribosomes in prokaryotes are small, ribosomes in eukaryotic are large.
  3. Prok are always unicellular. eukaryotic are often multicellular.
  4. Prok does not have nucleus or any membrane-bound organelle, eg mitochondria
  5. Prok DNA is circular, without proteins. Euka DNA is linear and associated with proteins to form chromatin.
  6. Prok have motility by rigid rotating flagellum made of flagellin. Euka cells have motility by flexible waving undulipodium, made of tubular.
  7. Prok cell division = binary fission. Asexual reproduction. Euka = mitosis/meiosis. Reproduction is asexual or sexual.
  8. Prok have a huge variety of metabolic pathways. Euka have common metabolic pathways.
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146
Q

How was the Tabacco Moisaic Virus discovered?

A
  1. Filter sap (bacterial-proof filter)
  2. Apply sap to healthy plant
  3. Agent multiplied only in cells that were dividing = virus
  4. Plant becomes infected.
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147
Q

What are viruses?

A

Acellular microorganisms that cannot survive without a host: no metabolic abilities of their own.

  • rely completely on biosynthetic machinery of infected cell to multiply.
  • hijack to use ribosome and polymerases to make protein and DNA and assemble to make more viruses
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148
Q

What types of cells can viruses infect?

A

All types (animal, plant, bacterial) - obligate intracellular parasites.

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149
Q

How many viruses on are Earth?

A

10^31

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150
Q

Size of viruses

A

10 - 400nm

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151
Q

Virus can have different shapes

A

Diagram.

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152
Q

Virion

A

when viruses exist in the form of independent particles.

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153
Q

Parts of a virion (2-3)

A
  1. genetic material made from either DNA or RNA
  2. a protein coat - capsid- which surrounds and protects the genetic material
  3. in some cases, an envelope of lipids that surrounds the protein coat when they are outside a cell.
    - envelope may have glycoproteins on the outside.
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154
Q

What is a nucleocapsid

A

Nucleic acid genome (RNA or DNA) surrounded by a protein coat (capsid)

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155
Q

What are capsids made of

A

Multiple units of the same building block known as PROTOMERS

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156
Q

3 types of symmetry promoters could be arranged in

A
  • helical eg TMV
  • icosahedral eg Adenovirus
  • complex eg bacteriophage
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157
Q

Describe the structure of icosahedral capsid

A

20 faced polyhedron. Each face = equilateral triangle.

  • each triangle has 3 subunits: capsomers
  • each capsomer has 5 (pentagon) protomer
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158
Q

Describe the viral genome

A
  • RNA or DNA
  • linear, circular, or segmented.
    All four possible forms of RNA and DNA are found in viruses: single and double stranded RNA and DNA
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159
Q

Massive number of variation in number of nucleotides in viral genome

A

4000 to >1 million nucleotides.

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160
Q

What do viruses infect?

A
  • all cell types: Euka and proka

- infect all forms of life i.e. animals, plants, bacteria, fungi, algae.

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161
Q

Define host organism:

A

An organism a virus infects.

- specific receptors recognised by virus

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162
Q

Define host cell

A

A cell a virus multiplies in

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163
Q

Basic viral life cycle in a host cell

A
  1. Attachment of vision to host cell.
    - lock and key
    - specific receptors
  2. Entry of nucleocapsid to host cell
  3. Synthesis of viral components i.e. genome and proteins
    - new capsid protein
    - replicate genome
    using host machinery, in cytoplasm.
  4. assembly of viral components into progeny
  5. release of progeny visions from host cell.
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164
Q

Another word for lytic

A

Virulent cycle

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165
Q

Another word for lysogenic

A

Latent/temperate

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166
Q

2 types of infections from prokaryotic cells

A
  1. lytic/virulent

2. lysogenic/temperate.

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167
Q

Draw the lytic cycle of phage infection

A
  1. Attachment
  2. Entry of phage DNA and degradation of host DNA
    - capsid does not enter cell
    - DNA injected into cell
    - viral DNA degraded by viral DNA = no replication of bacterial DNA
  3. Synthesis of viral genomes and proteins
    - no host DNA = viral DNA replicated
  4. Self-assembly (of head, tail and tail fibres)
  5. release
    - burst size (100-200 virions)
    - viral makes lysosome and holisons punch hole in membrane
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168
Q

Define lysogeny

A

the relationship between the temperate phage and host bacterium

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169
Q

Define prophage

A

the form of phage harboured in lysogen, which is simply the phage genome.

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170
Q

Compare the virulent life cycle of a bacteriophage and the latent life cycle of bacteriophage

A

.

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171
Q

Where is the prophage?

A

Either integrated into lysogen’s genome or remains free in the cytoplasm.

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172
Q

Draw the lysogenic cycle of infection.

A
  1. Phage DNA integrates into bacterial chromosome
  2. Bacterium reproduces normally, copying the prophage and transmitting it to daughter cells.
    - every time the bacteria DNA
    - due to integration, viral genome = silent. No transcription of viral genes. = stable lysogen
  3. Daughter cell with prophage
  4. Prophage exits the chromosome.
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173
Q

How is the lysogenic cycle induced to a lytic cycle?

A
  • change in culture conditions

- UV irradiation

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174
Q

What happens when the prophage is induced to become a virulent phage?

A
  • DNA becomes circularised

- lytic cycle commences

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175
Q

Draw diagram of lytic and lysogenic cycle

A

.

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176
Q

Outline Replication cycles of naked virus (no cell envelope)

A
  1. Entry and uncoating
    - recognise specific receptors on host cell surface
    - endosome or vesicle
    - enters by endocytosis
    - uncoats once in cell
    - end up with viral DNA and proteins.
  2. Replication
    - Host machinery replicates viral DNA = more viral DNA to make more virus
  3. Transcription and manufacture of capsid proteins.
    - DNA turned into mRNA
    - use mRNA to make capsid proteins.
    - mRNA made by host enzymes.
  4. Self-assembly of new virus particles and their exit from the cell.
    - probably by cell lysis
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177
Q

Outline replication cycle of RNA enveloped virus (eg HIV)

A
  1. Glycoproteins on the viral envelope bind to specific receptor molecules on the host cell, promoting viral uptake by the cell.
    - fuse with host cell membrane
    - not endocytosis
    - recognise receptor
    - some envelope viruses enter the host cell by fusion of the envelope with the cell’s plasma membrane; others enter by endocytosis.
    - for all enveloped RNA viruses, formation of new envelopes for progeny viruses occurs by the process below:
  2. The capsid and viral genome enter the cell. Digestion of the capsid by cellular enzymes releases the viral genome.
    - release of RNA and proteins
  3. The viral genome functions as a template for synthesis of complementary RNA strands by a viral RNA polymerase
    - the single-stranded RNA genome that functions as a template for synthesis of mRNA
    - reverse transcriptase makes DNA from RNA
    - number of cycles depend on how many RNA molecules (eg 2 RNA molecules for HIV)
  4. New copies of viral genome RNA are made using the complementary RNA strands as templates.
    - DNA inserted into chromosome for life
    - never leave the host genome -> PROVIRUS
  5. Complementary RNA strands also function as mRNA, which is translated into both capsid proteins (in the cytosol) and glycoproteins for the viral envelope (in the ER and Golgi apparatus).
  6. Vesicles transport envelope glycoproteins to the plasma membrane
  7. A capsid assembles around each viral genome molecule
  8. Each new virus buds from the cell, its envelope studded with viral glycoproteins embedded in membrane derived from the host cell.
    - budding means host cell not killed
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178
Q

Difference between provirus and prophage

A

Provirus -> DNA integrated into host genome. Unlike prophage, it remains FOREVER. Whereas prophage can become virulent.

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179
Q

What type of virus is HIV?

A

Retrovirus
- because they are RNA viruses, so must undergo retrostep.
Must convert RNA to DNA to mRNA

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180
Q

Describe the term viral latency in relation to the replication of bacterial and mammalian viruses

A

Viral latency = dormant, but can be activated.

Herpes simplex
- acute and latent infection
- DNA in nerve ganglion as a lysogenic virus - immune system can’t see
- acute phase results in blister formation
- virus retreats to nerve cells during latency
stressful stimuli (fever, trauma, emotional stress) and hormonal changes can reactivate the virus -> triggers reproduction.

Chickenpox (acute and latent)

  • acute disease in childhood, begins as a rash progressing to vesicles (blisters)
  • the virus remains latent in the body, can get activated and cause shingles during childhood.
  • carry DNA for life.
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181
Q

Is shingles transmissible

A
  • can’t transfer shingles to another person who has had chickenpox before. But if get shingles, can infect a person who hasn’t had chickenpox and give them chickenpox (not shingles).
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182
Q

Replicative cycle of HIV

A
  1. the envelope glycoproteins enable the virus to bind to specific receptors on certain white blood cells
  2. the virus fuses with the cell’s plasma membrane. The capsid proteins are removed, releasing the viral proteins and RNA.
  3. reverse transcriptase catalyses the synthesis of a DNA strand complementary to the viral DNA
  4. reverse transcriptase catalyses the synthesis of a second DNA strand complementary to the first
  5. the double-stranded DNA is incorporated as a provirus into the cell’s DNA
    - unique to retroviruses.
  6. Proviral genes are transcribed into RNA molecules, which serve as genomes for progeny viruses and as mRNAs for translation into viral protein (capsid and envelope)
  7. the viral proteins include capsid proteins and reverse transcriptase (made in the cytosol) and envelope glycoproteins (made in the ER)
  8. Vesicles transport the glycoproteins to the cell’s plasma membrane
  9. capsids are assembled around viral genomes and reverse transcriptase molecules
  10. new viruses, with viral envelope glycoproteins, bud from the host cell. (fuse with membrane)
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183
Q

What is the role of a membrane

A

To provide social conditions within the cell and keep them different to what’s outside

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184
Q

What must a cell do?

A
  • manufacture cellular materials (biological macromolecules)
  • obtain raw materials ( to make biomolecules)
  • remove wastes generated from production
  • generate the required energy to remove waste and build molecules
  • control all of the above
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185
Q

Why need organelles?

A

A cell must carry out many different processes that

  • require different conditions (eg catabolic vs anabolic) that
  • need separate compartments
  • called organelles
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186
Q

Functions of organelles

A
  • Provide special conditions for specific processes
  • keep incompatible processes apart
  • allow high concentrations of substances
  • form concentration gradients (some things only happen due to diffusion gradients)
  • package for transport or export
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187
Q

3 membranes

A
  • plasma membrane
  • mitochondrial membranes
  • nuclear envelope
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188
Q

Function of membranes

A
  • provide a semi-permeable barrier, so control movement of substances.
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189
Q

2 major components of phospholipids

A

Hydrophilic phosphate heads and hydrophobic fatty acid chain tails

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190
Q

What is membrane fluidity affected by

A

The composition of fatty acids

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191
Q

What makes a membrane viscous

A

Saturated tails pack tightly together

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192
Q

What makes a membrane fluid

A

Unsaturated tails prevent packing due to kinking due to double bonds.

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193
Q

How does cholesterol affect membrane fluidity

A

Cholesterol reduces membrane fluidity at moderate temperatures but increases fluidity at low temperatures
- regulate fluidity.

Therefore, at body temperatures, membrane fluidity is reduced by the presence of cholesterol

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194
Q

What are peripheral proteins

A

A kind of protein that is attached to the plasma membrane but not span all the way through it

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195
Q

What are membrane associated proteins

A

Proteins that span from one side all the way through the membrane to inside of the cell

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196
Q

Which substances move across membrane by diffusion

A
  • membrane permeable to lipid soluble (hydrophobic molecules) eg steroid hormones, gasses.
  • movement down conc grad.
  • eg O2, CO2, steroid hormones
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197
Q

Which substances move across membrane by facilitated diffusion

A
  • movement of hydrophilic molecules require membrane proteins
  • movement of specific substances down their conc grad
  • involves channeled or carrier proteins
  • no E input - passive.

eg water, glucose, ions

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198
Q

3 types membrane channels

A
  • ungated
  • voltage-gated
  • ligand-gated
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199
Q

eg of Ungated membrane channels

A

A few types of ion channels are ungated, meaning they are open all the time. For instance, some K+ and some Cl- channels are ungated. By contrast, Ca++ and Na+ ion channels are NEVER ungated.

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200
Q

Voltage-gated channels

A

Voltage-gated ion channels open or close in response to changes in membrane potential. Voltage-gated ion channels are key in the generation of electrical signals in nerve, muscle, and cardiac cells. See the web page describing an important example, the voltage-gated Na+ channel.

  • allow ion fluxes
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201
Q

eg of ligand-gated channels

A

Ligand-gated ion channels are opened when regulatory molecules bind to the channel protein. Many neurotransmitter receptors are ligand gated ion channels. An example is the nicotinic acetylcholine receptor. This is the receptor that is found at the neuromuscular junction on skeletal muscle cells, and also at synapses in autonomic ganglia.

  • open in response to an extracellular signal
  • bind to open eg hormones, neurotransmitters
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202
Q

Define active transport

A

The movement of specific substances against their conc gradient, requiring E input in the form of ATP and involving pumps

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203
Q

Types of active transport

A
  • may be direct or indirect

- uniport, co-transport, antiport

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204
Q

Describe uniporter

A

A transporter than only transport one type of molecule at a time

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205
Q

Describe symporter/co-transport

A

Move two or more types of molecule in the same direction through a membrane.

  • sucrose moved against conc grad
  • H+ and sucrose bind to protein at the same time
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206
Q

Describe antiporters

A

Transporters that move two different types of molecule in opposite directions at the same time.

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207
Q

Primary and secondary active transport

A

Somtimes, AT of one type of solute crates a cow grad that drives the passive transport of another solute.

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208
Q

Disease for defect in K+ channel

A

Epilepsy

- neutrons get too excited

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209
Q

Defect in tyrosine transporter

A

Albinism (type 2)

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210
Q

Defect in Cu2+ and Ag+ transporter

A

Wilson’s disease

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211
Q

Defect in Cl- channel

A

Cystic fibrosis

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212
Q

What are the two roles of membrane proteins

A
  • transporters

- give the cell its character

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213
Q

Functions of membrane proteins (6)

A
  • transport
  • enzymatic activity
  • signal transduction
  • cell-cell recognition
  • intercellular joining
  • attachment to (linking of) the cytoskeleton and extracellular matrix (ECM)
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214
Q

Describe the transport function of membrane proteins

A
  • a protein that spans the membrane may provide a hydrophilic channel across the membrane that is selective for a particular solute
  • other transport proteins shuttle a substance from one side to the other by changing shape. Some of these proteins hydrolyse ATP as an energy source to actively pump substances across the membrane.
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215
Q

Describe the enzymatic activity function of membrane proteins

A

A protein built into the membrane may be an enzyme with its active site exposed to substances in the adjacent solution.
- in some cases, several enzymes in a membrane are organised as a team that carries out sequential steps of a metabolic pathway

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216
Q

Describe the signal transduction function of membrane proteins

A

A membrane protein may have a binding site with a specific shape that fits the shape of a chemical messenger, such as a hormone.
- the external messenger may cause the protein to change shape, allowing it to relay the message to the inside of the cell, usually by binding to a cytoplasmic protein

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217
Q

Describe the cell-cell recognition function of membrane proteins

A

Some glycoproteins serve as ID tags that are specifically recognised by membrane proteins of other cells.
- this type of cell-cell binding is usually short-lived compared to intercellular joining

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218
Q

Describe the intercellular joining function of membrane proteins

A

Membrane proteins of adjacent cells may hook together in various kinds of junctions, such as gap junctions or tight junctions.
- this type of binding is more long-lasting than that for cell-cell recognition.

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219
Q

Describe the attachment to the cytoskeleton and extracellular matrix function of membrane proteins

A

Microfilaments or other elements of the cytoskeleton may be non-covalently bound to membrane proteins, a function that helps maintain cell shape and stabilise the location of certain membrane proteins.
= proteins that can bind to ECM molecules can coordinate extracellular and intracellular changes.

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220
Q

Describe the structure of tight junctions

A

At tight junctions, the plasma membranes of neighbouring cells are very tightly pressed against each other bound together by specific proteins.

  • forming continuous seals around the cells, tight junctions establish a barrier that prevents leakage of extracellular fluid across a layer of epithelial cells.
  • eg tight junctions between skin cells make us watertight.
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221
Q

Describe the structure of desmosomes

A

Desmosomes function like rivets, fastening cells together into strong sheets.
- Intermediate filaments made of sturdy keratin proteins anchor desmosomes in the cytoplasm.
Desmosomes attach muscle cells to each other in a muscle

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222
Q

Describe the structure of gap junctions

A

Gap junctions provide cytoplasmic channels from one cell to an adjacent cell and in this way are similar in their function to the plasmodesmata in plants.
- gap junctions consist of membrane proteins that surround a pore through which ions, sugar, amino acids and other small molecules may pass.
Gap junctions are necessary for communication between cells in many types of tissues, such as heart muscle, and in animal embryos.

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223
Q

What is the endomembrane system

A
  • nucleus
  • sER
  • rER
  • Golgi
  • lysosome
  • Plants cells do not have lysosomes. Instead, they have another type of organelle called the vacuole. The large central vacuole stores water and wastes wastes, isolates hazardous materials, and has enzymes that can break down macromolecules and cellular components, like those of a lysosome. Plant vacuoles also function in water balance and may be used to store compounds such as toxins and pigments (colored particles).
  • cell membrane
  • vesicles
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224
Q

Functions of smooth ER (4)

A
  • metabolism of carbohydrates
  • lipid synthesis for membranes
  • detox of drugs and poisons (anything not part of nutrient intake eg red pigment in tomato)
  • storage of Ca2+ (which can be released in response to signals)
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225
Q

How sER can change

A
  • extensive sER in cells active in the processes that the sER carries out eg liver: intake. Digestive system goes through liver. i.e. cells are not alike
  • the amount of sER can be increased or decreased to meet demand.
  • eg ER grows in response to more drugs, meaning that take more drugs = break down drugs to a lesser amount, meaning have to take more drugs to get same effect
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226
Q

Functions of rER

A
  • involved in protein synthesis (proteins that are released from cells or for membranes)
  • secreted and membrane-bound proteins enter the lumen (interior) or the rER
  • processed via the endomembrane system.
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227
Q

Why is rER rough in appearance

A

Due to ribosomes

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228
Q

Where dos the synthesis of cytoplasmic proteins (proteins that stay in the cell) occur

A

On free ribosomes

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229
Q

What is a vesicle

A

A bubble of phospholipid membrane

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230
Q

Properties of the Golgi complex

A
  • series of membrane sacs and associated vesicles
  • has polarity: cis and trans
  • vesicles from Er arrive at the cis face
  • processed vesicles leave at the trans face.
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231
Q

Roles of golgi

A
  • GLYCOSYLATION of protein (add sugar to protein (to proteins that end up on cell surface) )
  • addition or modification of carbohydrates to proteins (eg proteins on cell surface: the sugar on them interact with water)
  • important for cell surface proteins.
  • take carbohydrates made on the sER and modify them
  • important for cell surface proteins
  • SORTING proteins
  • adds molecular markers to direct proteins to the correct vesicles
  • eg a special phosphorylated sugar (mannose 6-phosphate) identifies lysosomal enzymes
  • selective proteins
  • Direct vesicle trafficking
  • adds molecular tags to direct vesicles to the correct target compartment (on outside of vesicle)
  • such tags are often short proteins exposed on the vesicle surface
  • have specific amino acid sequences
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232
Q

What is the phosphorylated sugar that identifies lysosomal enzymes

A

mannose 6-phosphate

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233
Q

Important flow of direction of vesicles

A
  • retrieval tag
  • direct proteins BACK to ER or previous Golgi cistern
  • important to maintain compartment integrity and function.
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234
Q

What’s the important of tags that direct to secretory pathways

A

Important for release and surface expression (expression of proteins on surface)

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235
Q

Describe exocytosis

A
  • transports material out of the cell

- delivers material to the cell surface

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236
Q

Two pathways for exocytosis

A
  • constitutive pathway: ongoing, uncontrolled. Cells are releasing things constantly (eg proteins that make up ECF)
  • regulated exocytosis: very controlled. For hormones and neurotransmitters (which have to be released at exactly the right time)
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237
Q

Mechanism of exocytosis

A
  • vesicle fuses with membrane.

- things on the vesicle membrane ends up on the cell surface.

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238
Q

3 roles of Golgi

A
  • Glycoslyation
  • sorting proteins
  • direct vesicle trafficking
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239
Q

3 types of endocytosis

A
  • phagocytosis
  • pinocytosis
  • receptor-mediated endocytosis
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240
Q

Describe phagocytosis

A
  • uptake of food particles

- forms a phagocytic vacuole which is digested (using lysosomes)

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241
Q

Describe pinocytosis

A
  • non-selective uptake of solutes.
  • drinking of ECM and any particles in it.
  • molecules dissolved in liquid
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242
Q

Describe receptor-mediated endocytosis

A
  • collects and concentrates specific molecules (that may be at a low concentration) eg Low density lipoprotein (LDL)
  • eg cell wants triangles
  • build receptors that fit triangles
  • pulled into cell
  • far larger number of triangles than non-selective uptake
  • but still takes up some unwanted solutes
  • receptor that can hold onto wanted particles -> pull into cell.
  • more specific compared to non-selective.
  • would get a higher concentration of desired solute than non-selective

eg Low density lipoprotein (LDL) particles

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243
Q

Describe the endosome-lysosome pathway

A

When lysosome is first formed, it doesn’t function. However, when it fuses with the vesicle, it matures.

Lysosomes digest cellular materials, as they contain HYDROLYTIC enzymes.

They degrade proteins, lipids, carbohydrates and nucleic acids

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244
Q

What enzyme do lysosomes contain

A

Hydrolytic

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245
Q

What can lysosomes degrade

A

Proteins, lipids, carbohydrates, nucleic acids.

  • break down into constituent components.
  • eg amino acids make new proteins.
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246
Q

Two variations of endosome-lysosome pathways

A
  • digest unwanted intracellular materials (eg nonfunctional organelles)
  • digest endocytosed material
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247
Q

What is endosome-lysosome pathways important for

A
- Cell health
eg stop taking drug, so ER broken down -> surplus for requirements 
- break parts down and build new ones. 
- important in programmed cell death 
- whole cell destruction or autophagy)
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248
Q

Tay-Sachs disease

A
  • mental and physical deterioration
  • motor/ cognitive and “speech” defects
  • blindness, deafness and paralysis
  • enzyme missing in lysosome, meaning can’t break down a certain material -> build up in cells. eg neurons.
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249
Q

Major components of the cytoskeleton

A
  • microtubules
  • intermediate filaments
  • microfilaments
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250
Q

Function of cytoskeleton (5)

A
  • gives mechanical support to cells and maintains, or changes, its shape
  • Anchors or directs the movement of organelles and cytoplasm. Helps maintain position of organelles
  • controls movement of cilia, pseudopods or even contraction of muscle cells
  • mechanically transmits signals from the cell’s surface to its interior
  • interacts with motor molecules (proteins) that change shape to produce cellular movements.
  • helps maintain cell shape
  • unlike the body’s skeletal system the cytoskeleton rapidly disassembles and reassembles
  • allows changes in cell structure
  • the cytoskeleton is highly dynamic but still provides stability
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251
Q

How is the cytoskeleton unlike the body’s skeletal system

A

The cytoskeleton can rapidly disassemble and reassemble, thereby allowing changes in cell structure.
- the cytoskeleton is highly dynamic but still provides stability.

252
Q

What are microtubules made of

A

Tubulin subunits

253
Q

Function of microtubules

A
  • resist compression
  • provide cell motility: cilia or flagella
  • chromosome movements in cell division
  • organelle movements
254
Q

Where does the microtubules originate

A
  • may radiate out from an organising centre (centrosome)
255
Q

How does microfilament undergo whole cell movement

A

Cilia: “rowing-like” motion perpendicular to the direction of movement.
- when cells are fixed in place, the beating of cilia can move fluid past the cells.
eg lungs -> cilia beat = rubbish gets pushed up

256
Q

How do organelles move within the cell

A

The microtubules provides a path that the vesicles can move along
- ATP-powered motor proteins attached to organelles
- ATP for motor
- moved along by moto
- can thus transport vesicles to targets or damaged organelles from distant sites eg nerve terminals
eg to lysosomes to be broken down.

ATP -powered motor proteins can “walk” organelles along MT
- can thus transport vesicles to targets, or damaged organelles from distant sites eg nerve terminals eg to lysosome to be broken down.

257
Q

What are microfilaments made of

A

Double chain of actin subunits

- twisted rope

258
Q

Structure of microtubules

A

Hollow tube of tubular subunits

259
Q

Structure of microfilaments

A

Twisted rope (double chain of actin subunits)

  • forms linear strands and 3D networks (with the aid of branching proteins)
  • linear actin microfilaments support movement
260
Q

Role of microfilaments

A
  • resist tension
  • cortical network under plasma membrane helps maintain cell shape
  • provide a gel-like consistency to outer cytoplasm.
  • changes in cell shape
  • muscle contraction
  • cytoplasmic streaming in plant cells
    cell motility (as in amoeboid movement)
  • division of animal cells
261
Q

How are microfilaments arranged in muscle

A

In parallel with the motor protein myosin

262
Q

How do microfilaments support movement of non-muscle cells

A

Pull on one and resist tension of microtubules, can achieve movement of non-muscle cells.

263
Q

What are intermediate filaments made of

A
  • various proteins including keratins, vimentins and lamins
264
Q

What is the structure of intermediate filaments

A

Supercoiled into “cables”

- fibrous subunit (keratins coiled together)

265
Q

How does IM compared to MT and MF

A

IM is less dynamic than MT or MF, which can build quickly and collapse quickly. IM is more stable, which is important for maintaining cell shape
- IM’s less dynamic nature is why its used for nuclear lamina

266
Q

Function of IM

A
  • maintain cell shape
  • anchor organelles- nuclear lamina.
  • anchors nucleus and certain other organelles
  • formation of nuclear lamina.
  • neuronal processes (neurofilaments)
  • abundant in nucleus -> nuclear lamina
  • neuronal processes -> neurofilmanets
267
Q

What are the 3 types of cell junctions

A
  • tight junctions
  • desmosomes
  • gap junctions
268
Q

Describe tight junctions

A
  • neighbouring cells tightly pressed together.

- may form a continuous seal

269
Q

Purpose of tight junctions

A

Prevent movement of fluid across cell layers

eg don’t want all crap from small intestine into blood supply
- select what it needs

270
Q

Describe desmosomes

A
  • anchoring junction: holds cells tightly tog, anchoring them
  • attachments between sheets of cells eg muscle
  • eg pull on muscle -> ind muscle cells contract -> all cells need to move together to turn into movement of the arm
  • lock together by desmosomes
  • hold hold onto the next
271
Q

Purpose of desmosomes

A

Act like rivets

  • a torn muscle is a torn desmosome
  • Pull on muscle = muscle cells contract -> all cells need to lock together-> locked by desmosomes -> cells hold onto next
272
Q

What are the fibres extending from the desmosomes

A

intermediate filaments.

- connect desmosomes into the rest of the cell

273
Q

Describe gap junctions

A

a point of cytoplasmic contact between cells

274
Q

Function of gap junctions

A
  • ions and molecules may pass from cell to cell

- allow rapid intercellular communication

275
Q

What is ECM composed of

A
  • material secreted by cells (fibroblasts) via constitutive exocytosis (constitutive type: ongoing and continuous). Fibroblasts are specialised to make ECM
  • mainly glycoprotein (rER then Golgi)
  • most abundant glycoprotein is collagen.
276
Q

What is the most abundant glycoprotein

277
Q

Properties of collagen fibres in ECM

A
  • great tensile strength
  • cable-like
  • approximately 50% of total body protein
  • like other proteins, collagen is “turned over” and must be replaced.
278
Q

How many % of total body protein is collagen

279
Q

Disease due to lack of vitamin C

280
Q

What does a lack of vitamin C result in

A

A failure of collagen synthesis. (after collagen breaks down, it’s not replaced)

  • hydroxyproline amino acids not formed
  • collagen fibres cannot cross-link correctly.
281
Q

What are proteoglycans

A

Proteins with extensive sugar additions

282
Q

Where is collagen embedded in

A

A proteoglycan matrix

283
Q

Why is proteoglycan important in ECM

A
  • traps water, therefore:

- resists compression and retains shape.

284
Q

How is there a pathway from outside of the cell to inside?

A

Other glycoproteins (fibronectins) attach cells to ECM

  • membrane proteins (integrins) link ECM to cytoskeleton
  • a communication link from ECM to the cell interior
285
Q

How do microtubules allow whole cell movement

A

Microtubules make up the core of flagella and cilia. They are arranged so that motor proteins can move along the microtubules and cause the flagellum/cilium to bend and change shape, thus propelling the cell.
- If the cell is fixed in position, then the movement of the cilia can cause fluid to move like they do in the lining of the respiratory tract.

286
Q

Why does a cell need energy?

A

To do work:

  • make new materials (bio molecules - many polymers: nucleic acids, proteins etc)
  • growth and replacement (need new materials) eg for cell division
  • movement: whole body (muscle) and within cell (transport) - eg neutrophil -> cytoskeleton etc Trackways inside cell for vesicles
  • pumping substances across membranes: accumulating materials (receptor-mediated endocytosis) and generates gradients (moving ions from one side to other. Pumped). Cotransport
287
Q

What are the two types of movement possible for a cell

A
  • whole body eg muscle

- within the cell (transport)

288
Q

Why does a cell need to pump substances across membranes?

A
  • to accumulate material (receptor-mediated endocytosis -> use E to generate vesicle)
  • generate gradient: moving ions from one side to other
  • cotransport
289
Q

Example of co-transport

A
  • active transport of H+ outside of membrane into a higher concentration
  • as H+ diffuse back in, it picks up sucrose, which is co-transported
290
Q

Where is the cell’s energy generated?

A
  • cytosol: glycolysis
  • mitochondria: citric acid cycle
  • mitochondrial membranes (oxidative phosphorylation)
  • Organelles are important as they allow different conditions for different reactions to occur.
291
Q

How is the cell’s energy generated?

A
  • cellular respiration
  • releases the chemical energy stored in food
  • converts this into small (useable units)
  • carried by the energy transfer molecule ATP
292
Q

How long is mitochondria?

293
Q

How many mitochondria are there per cell?

A

1 - thousands

294
Q

What does the number of mitochondria in a cell depend on

A

Energy demand due to cell type and function

295
Q

Structure of mitochondria

A
  • enclosed by two lipid bilayers
  • membranes contain special proteins
  • inner membrane highly folded -> cristae
  • contains mitochondrial DNA and ribosomes
  • produce some but not all mitochondrial proteins
  • mobile within the cell: go where E is needed eg nerves (at cell body, where neurons need E)
  • can change shape, fuse or divide
  • may form branched interconnected networks in cell
296
Q

Can the mitochondria produce proteins

A

Can produce some but not all

- contains mtDNA and ribosomes

297
Q

Can the mitochondria change shape, fuse or divide

298
Q

Is the mitochondria mobile within the cell

299
Q

The mitochondria may form branched interconnected networks in the cell

300
Q

What process happens in the cytosol (for respiration)?

A

Glycolysis

301
Q

What is glycolysis

A
  • reduces glucose into smaller units (pyruvate) (by the time take to get to cells, converted into glucose)
  • releases some energy (2ATP/glucose)
  • transfers electrons to the electron carrier NAD (which becomes NADH)
302
Q

What are mitochondrial compartments important for?

A

Energy generation

303
Q

What process takes place in the matrix of the mitochondria?

A

Kreb’s Cycle

304
Q

Describe the Kreb’s cycle

A
  • processes pyruvate
  • releases more energy (2 ATP/glucose)
  • transfers more electron to NAD and FAD
305
Q

Why have organelles (for respiration)?

A

Concentrate enzymes and substrates

to generate a concentration gradient and use this to power ATP formation

306
Q

What does NAD and FAD turn into once they receive electrons?

A

NADH and FADH2

307
Q

What process happens in the inter membrane space?

A
Oxidative phosphorylation ( electron transport and chemiosmosis)
- releases more energy (26-28 ATP/glucose)
308
Q

Describe the process in the ETC

A

ETC:

  • proteins in the inner membrane pump out protons
  • pump didn’t use all the Energy. Some left.
  • electron is passed to next pump.
  • next protein pumps H+
  • Next pump pumps out H+
  • H+ pump created a gradient.
  • electron is combined with O2 (H2O produced)

Chemiosmosis:

  • As H+ flow back into the matrix, it goes down the ATP synthase channel
  • turn the rotor around using the energy of flowing down concentration gradient.
  • ATP is produced (from attaching P to ADP).
309
Q

Where is the high concentration of H+ in mitochondria?

A

Intermembrane space

310
Q

Where is the high concentration of H+ in chloroplasts?

311
Q

Why does a cell need energy?

A

To do work:

- chemical, transport or mechanical work (movement of cell or whole organism)

312
Q

How is work achieved in the cell

A

Through E coupling

313
Q

What are exergonic reactions

A

Release E -> heat, light

314
Q

What are endergonic reactions

A

Absorb E eg building biological molecules/polymers

315
Q

What is energy coupling

A

When an exergonic reaction drives an endergonic reaction

316
Q

What provides the Energy coupling mechanism

A

ATP

  • captures E from exergonic reaction
  • transfer E to drive endergonic reaction.
317
Q

What is ATP involved in (3)

A
  • E transfer
  • RNA synthesis: build nucleotides
  • Neurotransmission: neurons send ATP messages to other neurons. ATP released from one neutron goes across synapse and communicates.
318
Q

How does ATP transfer E

A
  • 3 phosphates in a row.
  • neg charge on phosphate don’t like being pushed together
  • need to put lot of E to put 3rd O in
  • break down -> get E back
  • put a lot of E to make, break -> get lot of E back
319
Q

What type of reaction is ATP hydrolysis

A

Exergonic

- most E released when end phosphate breaks off -> ADP

320
Q

Are P-P-P bonds relatively large

321
Q

What type of E does ATP mainly generate

A

Heat

eg shiver -> muscle contract. Lost ATP -> Heat E released.

322
Q

What does ATP hydrolysis require

A

Water

  • when ATP hydrolyses, it releases E
  • high E bond
323
Q

How is coupling achieved

A

Through the transfer of phosphate: coupling speeds up.

  • forms a phosphorylated intermediate from donating a P from ATP.
  • the intermediate may be more reactive and therefore will react with the other reactant.
324
Q

How does the phosphorylated intermediate speed up a reaction

A

eg Glutamic acid and NH3

  • if just put with NH3, nothing happens
  • ATP makes it happen by transferring phosphates
  • creates a more reactive intermediate -> allows reaction to proceed.
  • the phosphorylated intermediate has more E (is unstable) than Glutamic acid and therefore are more likely to react with NH3.
325
Q

When ATP binds to a protein, what can it do?

A

ATP forms a phosphorylated intermediate which may change the shape of the molecule, therefore:

  • allows active transport of molecules
  • allows molecular movement to occurr
  • ATP puts PO43- on protein -> causes a change in shape.
  • eg one end open -> other end. Molecule move from one end to the other.
  • eg motor protein walk along MT, carrying a vesicle.
    PO43- on motor protein = change shape, moves one part of the molecule forward. Shuffles forward. Keep putting more on = another part shuffles forward = walking.
326
Q

How many ATP molecules does a single muscle cell use

327
Q

Is ADP + P -> ATP an endergonic or exergonic reaction

A

Endergonic

328
Q

Where does the energy to ADP + P -> ATP come from?

A

Cellular respiration

329
Q

2 ways cells get E out of food

A
  • fermentation: catabolism without O2
  • aerobic respiration: catabolism with O2: last stage of ETC: tale e-.
  • some prokaryotes substitute for O2 (with S)
330
Q

How may electrons move in a redox reaction

A

Movement of electrons within a molecule

  • eg if electron move away from C = CH4 has been oxidised
  • eg if electrons move closer to O, O has been reduced
331
Q

Energy involved in electron movement in redox

A
  • E is required to pull electron away from the positive atomic nucleus: E used to keep away electron away from positive charge
  • during reduction, electron move nearer to the O2 molecules therefore releasing E (from bonds) (E no longer needed)
  • This is the energy the cell captures and puts to work
332
Q

How does cellular respiration harvest E

A

Respiration harvests E in C-H bonds in food molecules by transferring the electron to O2 -> closer to nucleus = E released as the energy is lower.
- repositioning of electron in bonds

333
Q

Which bond does respiration harvest energy from

334
Q

Why do we respire rather than combust food

A

Simple combustion generates too much heat.

335
Q

What’s the process of respiration oxidation like

A

A series of controlled steps

- electron stripped from glucose and transferred to NAD

336
Q

Which enzyme reduces NAD+

A

Dehydrogenase

337
Q

What does the dehydrogenase enzyme do?

A

removes 2 H atoms from glucose

  • transfers 2 electrons plus 1 H+ to NAD+ forming NADH (electron carrier)
  • NADH used to power ETC
338
Q

How many electrons and H+ are transferred to NAD+ by dehydrogenase?

A

2 electrons plus 1H+

339
Q

What is NADH used for?

A

to power ETC

340
Q

Which two processes does oxidative phosphorylation encompass?

A
  • ETC

- Chemiosmosis

341
Q

Draw ATP synthase

342
Q

Components of ATP synthase

A
  • half channel
  • rotor
  • Stator
  • internal rod
  • catalytic knob
343
Q

What is ATP described as

A

Ion pump in reverse

344
Q

Pathway of H+ in ATP synthase

A
  1. H+ ions flow into a half channel
  2. H+ bind to the root and change its shape. The change in shape causes the rotor to turn (eg one notch around)
  3. Rotor spins
  4. After one turn of the rotor, H+ exit to the mitochondrial matrix
  5. rotor turns the rod which activates catalytic sites to produce ATP.
345
Q

Why can’t H and O2 just react in one step

A

too much energy
- explosive release of heat and light energy
- 2H (from food via NADH)
- 2 H -> 2H+ + 2e-
- electrons go through electron transport chain
- each protein pump produces some energy
2H+ + 2e- + O2 recombine to make H2O = controlled release of energy for synthesis of ATP

346
Q

How is NAD reduced

A

NAD + 2H (which is broken down to 2e- + 2H+)

  • NAD + 2e- + H+ -> NADH
347
Q

Most prominent organelle in the cell

348
Q

How big is the nucleus

349
Q

How many nucleus per cell in most cases

A

1

- except RBC and muscle

350
Q

Does the nucleus contain all of the cell’s genes

A

No. It contains most but there are some in mitochondria

351
Q

What does the nucleus store

A

Serves as a repository of genetic information

352
Q

Describe the structure of the nucleus

A

Surrounded by nuclear envelope
- composed of TWO membrane, each membrane is a phospholipid bilayer

Inner surface of nuclear envelope lined by nuclear lamina -> protein
- composed of IF -> cable-like, tough, bit of flexibility, built to last

353
Q

How many membranes are there in the nuclear envelope

354
Q

What is the inner surface of the nuclear envelope lined by?

A

Nuclear lamina

355
Q

What is the nuclear lamina composed of?

A

IF

- cable-like, tough, bit of flexibility, but to last

356
Q

Function of nuclear lamina

A
  • helps maintain shape of the nucleus

- organises the packing of DNA -> anchor points in which DNA is structured

357
Q

What is the disease due to defective nuclear lamina

A

Hutchinson-Gilford Progeria syndrome

  • cell nuclei have abnormal shape
  • results in accelerated again
  • can’t use DNA properly -> can’t cell div properly therefore can’t replace old cells that die off
358
Q

What is transported out of nucleus

A

mRNA, rRNA, tRNA

- need to get info from nucleus to outside to make proteins

359
Q

What is transported into the nucleus

A

Control signals from other cells
- eg growth factors, hormones

Energy and materials

  • raw materials: nucleotides for making RNA -> Need ATP to make RNA etc
  • proteins needed for transcription
  • proteins needed for chromosome replication
360
Q

What do nuclear pores act as

A

Regulated mechanisms -> gates

- so that repository of genetic information is protected

361
Q

How long is DNA in human cell

362
Q

How must DNA be organised

A
  • well packed

- but also ACCESSIBLE (to turn into mRNA etc)

363
Q

What are chromatin fibers

A

After DNA double helix is combined with histone proteins

364
Q

First step of DNA organisation

A

DNA double helix is combined with histone proteins to form chromatin fibres.
- chromatin fibres undergo multi-level packaging.

365
Q

What is the structure called after DNA double helix is wound around histone proteins (bead)

A

Nucleosome

366
Q

What is a nucleosome

A

After DNA has wound around histone protein (each bead)

367
Q

Diameter of DNA double helix

368
Q

Which histone proteins do the helix interact with first

A

H2, H3, H4

369
Q

What is the diameter of nucleosome

370
Q

Why does DNA wrap around histone proteins

A

to ensure accessibility by twisting around histone

371
Q

2nd Step of DNA organisation around wrapping around H2-H4

A

Further interactions between DNA and H1

- causes 10nm fibre to coil to form 30nm fibre

372
Q

Diameter of the fibre after interaction with H1

373
Q

3rd stage of DNA organisation

A

30nm fibre loops to form 300nm fibre

- coiled in an organised way

374
Q

Diameter of fibre after 3rd stage of DNA organisation

375
Q

4th stage of DNA organisation (during metaphase)

A

During cell div, 300nm fibres coil to form metaphase chromosomes during METAPHASE
- pack into a transportable form so can send to one cell or another

376
Q

Chromatin

377
Q

Why is the DNA packed into chromosomes during cell div?

A

pack into a TRANSPORTABLE form so can send to one cell or another

378
Q

Interphase

A

between cell divisions

379
Q

Euchromatin

A

less dense

  • appear light on EM
  • often genetically active = DNA that the cell is using at that time
  • genes for cell function are active
380
Q

Heterochromatin

A
  • dense
  • genetically inactive
  • certain genes “switched off”/not expressed
    eg neutrophil vs neuron
  • neutrophil need components to phagocytose bacteria, whereas neurons need to turn on genes to make neurotransmitter
381
Q

What happens to chromatin during interphase

A

Some regions of chromatin are more compact than others during interphase

  • euchromatin
  • heterochromatin
382
Q

What type of relationship exist between euchromatin and heterochromatin?

A

DYNAMIC

  • eg during cell div, need genes that allow cell div
  • after cell div, don’t need so get packed into heterochromatin until needed again, where it is then unfolded into euchromatin
383
Q

Is the location of chromosome within the nucleus random

A

NO

  • not random
  • stay organised due to interaction/hooking onto with nuclear lamina
384
Q

What happens to chromosomes in cancer cells

A

Loss control of chromosomes

  • genes mixed up
  • genes from different chromosomes on different chromosomes
385
Q

2 parts of a plant cell

A

cell wall and protoplast

386
Q

Main differences between animals and plants

A

Animals are heterotrophic

  • rely on plants indirectly (Carnivore) or directly (herbivore) for food
  • mobile

Plants are autotrophic

  • immobile
  • have to cope with the environment they are in
  • make their own food
387
Q

Function of cell wall

A
  • protection -> against eg fungi

- structural support - enables leaves to present to maximise photosynthesise

388
Q

One problem of having a cell wall

A

Communication

- solved by plasmodesmata

389
Q

What is a vacuole

A

an organelle surrounded by a single membrane -> one phospholipid bilayer -> tonoplast

390
Q

Tonoplast

A

membrane of vacuole

391
Q

How many vacuoles do plant cells have

A

Mature plant cells typically have a single large vacuole

- young plant has many small vacuoles

392
Q

How does the vacuole affect the position of organelles

A

Push all organelles to between the plasma membrane and tonoplast
- pushed against cell wall

393
Q

Where is the tonoplast produced

A

by the golgi associated ER

- membrane broke off -> budding off of Golgi ass

394
Q

3 functions of vacuoles

A
  1. storage
  2. breakdown of macromolecules
  3. regulation of cell turgor -> rigidity of plant cells
395
Q

What are the two types of metabolites that the vacuole stores

A

Primary metabolites - growth associated

Secondary metabolites - not growth associated

396
Q

Which type of metabolites are growth associated

397
Q

Examples of primary metabolites

A
  • inorganic ions (Ca2+, K+ eg cofactor for enzymes)
  • organic acids
  • sugars (glucose, polysaccharides, eg oligosaccharides)
  • amino acids
  • proteins
  • lipids
398
Q

Can different types of cells have different ratios of primary metabolites

A

yes.

- eg more lipids in seedlings as it is used as an energy source to drive germination

399
Q

What type of membrane is tonoplast

A

SELECTIVE

  • controls movement of substances into and out of the vacuole
  • some molecules such as water can pass in and out freely (for turgour pressure)
400
Q

How is the tonoplast selective

A

Proteins in membrane that transport certain substances

- regulate particular substances in and out

401
Q

Example of a substance that can pass freely through the tonoplast

A

Tonoplast

- for turgour pressure

402
Q

2 types of secondary metabolites

A
  1. molecules for defence
  2. molecules for signalling
    - eg pollinators to disperse fruit
403
Q

Where are secondary metabolites found

A

Secondary metabolites are specific to specific plants

- found in certain regions.

404
Q

Example of molecules for defence

A

Rubber tree
Rubber = a carbohydrate consisting of high molecular weight chains of 1,4-polyisopene residues
- specialised cells have small latex containing vacuoles -> deterrent for insects
- latex move into mouthpart.
- becomes more viscous on contact with O2
- makes mouth stick together

405
Q

2nd example of molecules for defense

A

Some specialised plaint cells have vacuoles containing raphides

  • raphides are needle shaped crystals of calcium oxalate
  • makes leaf less penetrable to silkmoth larvae
  • if the insect ingest it, it damages their digestive tract -> prevent eating more
406
Q

Group of nitrogen-containing bases

407
Q

What are most of the alkaloids produced from

A

amino acids

408
Q

3rd type of molecules for defense

409
Q

What are alkaloids

A

Group of nitrogen-containing bases

410
Q

Properties of alkaloids

A
  • have a variety of toxic effects on animals
  • eg humans -> target nervous systems
  • sequestered in sufficient conc to be effective (big hit -> kill insect)
  • found in vacuoles that the plant wants to protect the most eg cells of new tips
411
Q

Where are alkaloids found

A

in vacuoles of cells that the plant wants to protect the most eg cells of new tips

412
Q

How are vincristine and vinblastine produced commercially

A

Using cell cultures biotech

  • undifferentiated plant cells
  • when groups of undifferentiated cells grow together they are often leaky -> so secondary metabolites excreted into medium
413
Q

Why is using cell cultures to make pigments (vinblastine and vincristine etc) more efficient than extracting from harvested material

A
  • more efficient than extracting from harvested material as it degrades over time etc
  • ecologically less damaging
414
Q

What is nicotine used for

A

Insecticide. From tobacco plant

415
Q

Example of pigments that is anticancer

A

Vincristine and vinblastine

416
Q

Name of pigments (molecules for signalling)

A

Anthocyanins

417
Q

What is anthocyanins used for

A
  • attracting animals -> cross pollination -> genetic diversity. eg distribution of seeds when ripe
  • attract pollinators and animals to disperse seeds. eg blackberries -> more palatable. More black = more anthocyanins -> insect move away long enough to excrete it out.
418
Q

2nd function of vacuoles

A

Breakdown of organelles and macromolecules

- digestion of cytoplasmic constituents

419
Q

How does the vacuole breakdown organelles and macromolecules

A

Vacuoles are acidic and contain hydrolytic enzymes similar to lysosomal enzymes of animal cells

420
Q

Organelles and macromolecules that need to be broken down need to be transported into vacuole across tonoplast

A

Another reason why tonoplast is selective.

421
Q

What types of enzymes does the vacuole contain

A

Hydrolytic

422
Q

is the vacuole acidic or alkaline

A

Acidic -> for breakdown of substances

423
Q

3rd function of Vacuoles

A

regulation of turgour

- provides structural support

424
Q

How come the vacuole can regulate cell turgour

A

because they contain water and make up such a large portion of the protoplast, vacuoles can play a role in the regulation of cell turgor

425
Q

Does the vacuole have a neg or pos osmotic potential

A

High concs of solute (as it is a place of storage) in vacuoles have a negative osmotic potential, resulting in water uptake
- expands

426
Q

What is osmotic potential

A

The potential of water molecules to move from a hypotonic solution to a hypertonic solution across a semi-permeable membrane.

427
Q

What structure enables plant cells to take up water without bursting

A
  • plant cell wall
  • pressure from cell wall prevents bursting
  • plant cells build up a large internal pressure -> turgour pressure
428
Q

What does turgour pressure contribute to

A

Rigidity and structure

429
Q

When would the plant have a decreased turgour pressure

A

Loss of water from vacuoles

- if can’t move-> soil dry

430
Q

What does loss of turgour pressure result in

A

Wilting (dec cell size)

loss of structural integrity

431
Q

What happens to the cells when a plant loses turgour pressure/wilts

A

Dec cell size

  • plasma membrane pulls away from cell wall.
  • cell wall remains as before
432
Q

What happens when a wilted plant rehydrates

A

go back to original state

433
Q

What does wilting cause the leaves to be like?

A

Leaves turned away from light

- under water stress no photosynthesis -> damaging to capture high E light

434
Q

Key points about vacuoles

A
  • bounded by a single membrane - tonoplast
  • multiple small vacuoles in young cells
  • single larger vacuole in old cells
  • originates from golgi associated ER (reflected in the function of degradation of macromolecules -> enzymatic function)
  • 3 functions:
  • storage of primary and secondary metabolites
  • breakdown of organelles and macromolecules
  • regulation of cell turgor.
435
Q

Does the tonoplast have a single or double membrane

436
Q

How did the photosynthetic eukaryote come about

A
  1. Non-photosynthetic eukaryote
  2. engulfing of photosynthetic prokaryote. Bacteria maintained within rather than taking its carbohydrates. Internal source of energy -> mutualistic relationship
  3. chloroplast becomes a semi-autonomous organelle
  4. photosynthetic eukaryote

Chloroplast -> bacteria

437
Q

What does semi-autonomous refer to

A
  • divide independently of the cell but remain dependent on cell for most of their proteins
  • has own genome (circular DNA, mRNA, tRNA and ribosomes) and produces some of its own proteins
  • divide on their own in a sim way to binary fission
438
Q

How is the chloroplast DNA arranged

439
Q

Are all of the proteins that the chloroplast need encoded by chloroplast’s genes

A

Although ctDNA contains info for formation of many chloroplast proteins, some proteins (that are shuttled back in to the chloroplast) found in the chloroplast are encoded by genes present in the nucleus of the cell.
= reliant on host.
- some genes were transferred to host nucleus, so host has ultimate control.

440
Q

What is ATP used for

A
  • biosynthesis
  • AT (accumulation of materials and generation of gradients)
  • movement (whole body eg muscle, or movt of structures within cell)
  • bioluminescence
  • electrical work
  • growth (inc cell size) and repair
  • inc cell number (cell div)
  • differentiation (egg to ind)
  • to maintain order
441
Q

Not every cell need chloroplasts

A

in a multicellular organism

442
Q

4 types of plastids

A
  • chloroplasts
  • chromoplasts
  • leucoplasts
  • proplastids
443
Q

Function of chloroplasts

444
Q

Function of chromoplasts

A

synthesise and storage of coloured pigments (NOT anthocyanins)

445
Q

Where are anthocyanins

A

IN VACUOLE NOT CHROMOPLASTS

446
Q

Function of leucoplasts

A

storage of assimilates (starch)

- C compounds: carbohydrates

447
Q

Function of proplastids

A

precursors to other plastids

  • undifferentiated
  • can form any of the other plastids depending on cell its in.
448
Q

Features that the chloroplast has in common with mt

A
  • bounded by 2 membranes
  • contain nucleic acids
  • outer membrane highly permeable
  • inner membrane more selective -> needed for subcellular organisation
449
Q

How many membranes does a chloroplast have

A

2

- 2 phospholipid bilayers

450
Q

What is the unique feature of chloroplasts

A
  • 3rd membrane system -> light harvesting
  • lipid bilayer
  • grana and thylakoids
  • increased SA for capturing light
451
Q

Examples of large SA:vol ratio in plant

A

Leaf itself

thylakoid.

452
Q

Functions of chloroplasts

A
  • capture light energy (big SA) and convert it to chemical E
  • light reactions -> thylakoid membranes
  • Calvin cycle in storm
453
Q

What does light reactions produce

A
  • ATP and NADH

- energy as chemical E

454
Q

Where do light reactions occur

A

On thylakoid membrane

455
Q

Where do the Carbon fixation/dark reactions occur

456
Q
  • What does the Calvin cycle use
A

ATP and NADH

- fixing CO2

457
Q

Structure of chloroplasts

A
  • thylakoid stacked -> light harvesting

- lumen (inside each pancake) -> space in thylakoid -> thylakoid space. Accumulation of H+ -> diffuse down conc grad

458
Q

How big are chloroplasts

A

Plant chloroplasts are large organelles (5 to 10 μm long

459
Q

What are the 3 membranes of chloroplasts

A
  • inner
  • outer
  • thylakoid
460
Q

What are the 3 compartments of chloroplasts

A
  • stroma
  • thylakoid space
  • intermembrane space

These compartments and the membranes that separate them serve to isolate different aspects of photosynthesis

461
Q

Reactions of Calvin Cycle

A
  1. Carbon fixation.
  2. reduction
  3. regeneration
462
Q

How do deoxy and oxyribose differ

A

O on OH of C2

463
Q

how do carbohydrate function as energy sourcae

A

E storage polysaccharides

  • starch in plants (in starch granules) -> amylose and amylopectin
  • glycogen in animals
  • NOT cellulose
  • E source need to break glycosidic bonds ti sep glucose. Can only break alpha 1-4 bonds in our body. Can’t break beta1-4 bonds = can’t digest.
464
Q

How do carbohydrates function as structure

A

cellulose in plant

  • cell wall -> cellulose microfibrils in plant cell wall
  • long chain of glucose linked by beta1-4. H bonds between chains
  • cellulose provides dietary fibre.
465
Q

Mycoplasmas

A

Prokaryotes that lack cell walls

- live in isotonic environments and therefore not subject to osmotic pressure.

466
Q

What are prokaryotes that lack cell walls called

A

Mysoplasmas

467
Q

What does penicillan target/inhibit

A

Inhibits enzymes catalysing cross-linking of NAG NAM

- cross links not formed = cell wall weakened = cell lyses.

468
Q

Structure of bacterial cell wall

A

Carbohydrate backbone NAM NAG linked by peptide cross-bridge

469
Q

What does tumbling promote

A

Random rotational turns during swimming.

470
Q

How are the chemoreceptors in cytoplasm arranged

A

Hexagonal array.

471
Q

Parts of an endospore

A
  • exosporium
  • spore coat
  • core wall
  • cortex
  • DNA
472
Q

What’s the type of virus that can integrate the DNA synthesised from the viral RNA genome as a provirus into the host cell chromosomal DNA?

A

Retroviruses.

- a characteristic unique to retroviruses

473
Q

What happens to Herpes simplex during the latent phase

A

Lysogenic/latent virus
- viral DNA sits in nerve ganglia -> dorsal ganglia
- immune system can’t see
= no symptoms

474
Q

How is the Herpes Simplex virus reactivated

A

By stressful stimuli (fever, trauma, emotional stress)

- triggers replication of virus

475
Q

What is the acute phase of Herpes simplex

A

blister formation

476
Q

How do flagella work

A

The motor of a prokaryotic flagellum consists of a system of rings embedded in the cell wall and plasma membrane.

  • the ETC pumps protons out of the cell
  • the diffusion of protons back into the cell provides the force that turns a curved hook and thereby cases the attached filament to rotate and propel the cell.
477
Q

Differences between attachment of glycoprotein and glycolipid

A

Glycoprotein attaches to membrane protein. Glycolipid attaches to phosphate head of phospholipids.

478
Q

Integral protein

A

Penetrate the hydrophobic interior of lipid bilayer

479
Q

Function of peripheral proteins

A

eg released into the cell as a secondary messenger when the integral protein its bonded to changes shape.
- also enzymatic.

480
Q

Enzymatic activity of membrane proteins

A

A protein bult into the membrane may be an enzyme with its active site exposed to substances in the adjacent solution
- in some cases, several enzymes in a membrane are organised as a team that carries out sequential steps of a metabolic pathway.

481
Q

Drug example of smooth ER function

A
  • enzymes embedded in Er break up drugs eg liver eg painkillers
  • drugs arrive in blood stream. Goes into cells of liver
  • cells break down drug but still enough remaining to go to blood and then brain to dec pain
  • if not enough drug, take more. Same amount of enzyme means ER can’t cope so more left into blood.
  • ER grows in response. More enzymes. Take more drugs = break down into low levels = take more drug to deal with same pain to get same effect.
482
Q

Where do the secreted and membrane-bound proteins go after being made on the rER

A

Lumen of rER

  • go to gGolgi and then travel elsewhere
  • in vesicle = bubble of phospholipid membrane
483
Q

What are retrieval tags

A
  • direct proteins back to ER or previous Golgi cisternae to maintain compartment integrity and function.
484
Q

two types of tags for vesicles

A
  • retrieval tags

- other tags direct to secretory pathways (important for release and surface expression of proteins on surface)

485
Q

What is autophagy

A

Whole cell destruction

- important for programmed cell death.

486
Q

Diameter of MT

A

25nm with 15nm lumen

487
Q

Diameter of MF

488
Q

Diameter of IF

489
Q

Two things that the ATP-powered motor proteins can transport

A

Vesicles to targets

- damaged organelles from distant sites eg nerve terminals et to lysosome to be broken down.

490
Q

What is a torn muscle

A

A torn desmosome

- pulled desmosomes out from one cell to other

491
Q

Fibronectin

A

Fibronectin sometimes serves as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates

Fibronectin is a high-molecular weight (~440kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Similar to integrins, fibronectin binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans)

492
Q

What is the glycoprotein that anchors cells to collagen or proteoglycan substrates

A

Fibronectin

493
Q

How is collagen like other proteins?

A

Must be turned over and replaced

494
Q

What amino acid is not formed in scurvy

A

Hydroxyproline

495
Q

What do interns function as

A

a communication link from ECM to cell interior

496
Q

Difference between intern and integral proteins

A

Integrins are receptors (a specific category) which are responsible for cellular adhesion and in some cases, cellular signalling too.
- However, integral proteins are a generalised category which includes all sorts of transmembrane proteins like receptors, enzymes, signalling cascades, transporters, cellular adhesion domains etc.

497
Q

Which type of bacteria are fimbriae more commonly found on

498
Q

Structure of gap junctions

A

Gap junctions are plasma membrane spatial microdomains constructed of assemblies of channel proteins called connexins in vertebrates and innexins in invertebrates.

499
Q

Desmosome structure

500
Q

What do proplastids develop in response to light

A

Chloroplast

501
Q

Co-transport

A

Take H+ from inside and pump out -> requires E as moving up conc grad

  • want to get back in -> diffuse (facilitated). E produced used to piggy back sucrose
  • pick up sucrose
  • drags sucrose with it
  • can move in at same time.
502
Q

Protein complexes in ETC

A

Protein complex I, III, IV

503
Q

At which protein complex in mt ETC is water produced

A

Complex IV

504
Q

At which complex in mt ETC is NADH oxide to NAD+

505
Q

What happens at complex I in respiration in ETC

A

NADH -> NAD+

506
Q

What happens at complex IV in ETC in respiration

A

2H+ + 0.5O2 -> H2O

507
Q

What happens at each of the protein complexes in ETC

A

H+ pumped into intermembrane space

508
Q

What does oxidative phosphorylation compose of

A

ETC and Chemiosomosis

509
Q

Which stage of respiration produces NADH

A

Glycolysis and Krebs cycle

510
Q

In which stage is NADH oxidised

A

At protein complex 1 in ETC

511
Q

What are the pumps in mt and ct powered by

A

mt - electrons from food

ct - light E

512
Q

Darker layer between two plant cells

A

Middle lamella

513
Q

What is the middle lamella made of

A

Predominantly pectin

514
Q

What is pectin

A

A gel-like polysaccharide

- joins the cells together

515
Q

Which cell wall is the furthest away from the interior of the cell

A

Primary cell wall

516
Q

Whys is the primary cell wall the furthest from the interior of the cell

A

Because it is laid down first

- cell walls are laid down just outside plasma membrane

517
Q

What is wood

A

Secondary cell wall

518
Q

What makes cellulose highly ordered and strong

A

H bonds between glucose chains

519
Q

Is cellulose a High E carbohydrate

520
Q

What is the most abundant organic macromolecule on Earth

521
Q

What do cellulose form

A

Microfibrils

522
Q

What is the major component of primary and SECONDARY CELL WALL?

523
Q

What cells produce the primary cell wall

A

Young cells

524
Q

Properties of primary cell wall

A

Relatively thin and flexible

  • therefore the cells can still grow
  • push against cell wall- > rearrangement of cell wall as it expands
525
Q

Composition of primary cell wall

A
Cellulose 25-30%
Hemicellulose 15-25%
Pectin (absorbs water and gel-like) 35%
Protein 5-10%
- predominantly extensin
526
Q

What its the predominant protein in the primary cell wall

527
Q

What is the composition of cell wall

A

Two phases plus a network of extensin

528
Q

What is the crystalline microfibrillar phase made of

529
Q

What is the noncrystalline matrix made of

A

Pectic polysaccharides

Hemicellulosic polysaccharides

530
Q

What is hemicellulose

A
  • polysaccharide

- heterogenous = different sugars

531
Q

Difference between cellulose and hemicellulose

A

Cellulose just has glucose

Hemicellulose has other sugars

532
Q

Structure of hemicellulose

A

One type of sugar forming backbone
- other sugars forming side chains

Cross linking between cellulose and hemicellulose

533
Q

What is pectin’s structure

A

Zigzag

  • branched
  • negatively charged polysaccharides
  • bind water and have gel-like properties
  • gel-like properties also allows binding with cellulose
534
Q

What is extensin primarily involved with

A

Extensibility

- ability for the primary cell wall to expand as it grows

535
Q

How does extension affect extensibility

A

In a disorganised way when the cell wall is able to expand, eg phase of expansion. Push against microfibrils can slide against each other.

When stop growing/under stress conditions, cross-linking of protein with the cellulose

  • causes dehydration of cell wall
  • makes it much stronger and rigid.
  • not expandable
  • cells can’t grow in this stage.
536
Q

What happens when the plant cells stop growing/under stress conditions

A

Cross-linking of protein with cellulose

  • causes dehydration of cell wall
  • makes it much stronger and rigid
  • not expandable
  • cells can’t grow in this stage.
537
Q

How is the primary cell wall synthesised

A
  1. Cellulose microfibrils at plasma membrane
    - excreted by plasma membrane
  2. Polysaccharides (pectin and hemicellulose) in Golgi and transported to PM in vesicles.
    - fuse with PM, contents released (to where cellulose is produced)
  3. Cell wall proteins (extensions) from the rER
    - vesicle through Golgi, vesicle to PM and released.

Therefore immediately outside the plasma membrane = producing cellulose and secreting pectin, semi and extensins

538
Q

Where is cellulose synthesised

A

Plasma membrane

539
Q

Steps to forming cellulose

A

Sucrose = disaccharide

  • cleaved
  • take glucose

Protein complex SPANS plasma membrane
- two enzymes
sucrose synthase
cellulose synthase

Cellulose synthase bind glucose together and form chains of cellulose
- secreted into cell wall.

540
Q

Two enzymes in the plasma membrane complex for cellulose formation

A
  • sucrose synthase

- cellulose synthase

541
Q

Once cellulose is made, can the glucose be taken back

A

No.

Can’t degrade them.

542
Q

What does the arrangement of cellulose affect?

A
  • strength of the ell

- morphology of cell

543
Q

What is cellulose synthase associated with

A

Microtubules

544
Q

What affects where cellulose is laid down

A

Position of the microtubules
- MT = railway tracks that the cellulose synthase go across

  • MT on the inner surface of cell
  • Cellulose on outer
545
Q

What is the middle lamella high in

546
Q

Three functions of cell wall

A
  • Structural support and influences cell morphology.
  • protection: from pathogen attack eg fungi and bacteria
  • prevents excessive water uptake: regulation of turnout
547
Q

What must the plant cell defend itself from (protected by cellulose)

A

Pathogen attack from fungi and bacteria.

548
Q

How does the orientation of cellulose microfibrils influence cell morphology

A

Randomly oriented

  • the cell will expand equally in all directions
  • no pressure points, equal coverage
  • expand equally in all direction

Right angles to the ultimate long axis of the cell
- the cell will expand longitudinally along that axis

549
Q

What determines the shape of the cells

A

How the cellulose is laid down

How the cellulose is laid down is determined by the cytoskeleton

550
Q

What must the position of the cellulose allow for guard cells?

A

Come together in certain circumstances

551
Q

How does the cell wall serve its protective role

A

Cell wall acts as a protective barrier

- not just passive protection (but can be just passive)

552
Q

Example of cell wall acting as an active protection

A

Sorghum plant responding to fungal infection

  • red colour = response to infection
  • produce inclusion bodies that contain fungicide

Neighbouring cells sense neighbour’s pathogen attack

  • also produce fungicide
  • secreted into cell wall

Sensing and responding

553
Q

How does the cell wall regulate turgour pressure

A

The plant vacuole has a negative osmotic potential due to high conc of solutes
- water will enter the cell by osmosis into a higher osmotic potential

  • no cell wall = water continues to enter
  • presence of cell wall = pressure
  • pressure of protoplast pushing against cell wall
  • equal and opp forces so cell wall pushing against protoplast = no expand = no more water intake
    = no burst of cell
  • turgour pressure = riding cells
  • contributes to the structural support.
554
Q

Do all plant cells have a secondary cell wall

555
Q

When are secondary cell wall produced

A

After cell growth has stopped

556
Q

how do secondary cell walls compare to the primary cell walls

A
  • thicker and stronger than primary (no expansion)

- provides more structural support than primary eg wood is all secondary cell wall

557
Q

Structure of secondary cell wall

A
  • multiple layers (can lay down multiple layers of cellulose)
  • eg three layers of secondary cell wall. Really thick.
  • lay down secondary cell wall
  • undergo programmed cell death
    = hollow tubes
    = xylem cells.
  • microfibrils in each layer have different orientations
  • this strengthens the secondary wall
558
Q

How are the microfibrils oriented in the microfibrils in each layer f the secondary cell wall

A

microfibrils in each layer have different orientations

- this strengthens the secondary cell wall.

559
Q

Secondary cell wall chemical structure

A
  • More cellulose than primary
  • less pectin
  • 15-35% lignin
560
Q

Number one thing that limits processing of cell wall

561
Q

Second most abundant organic macromolecule

562
Q

What is the function of lignin in secondary well wall

A

Confers

  • strength
  • rigidity
  • hydrophobicity (innert, eg enzymes can’t activity as water can’t get in)
563
Q

Do different plants have different lignin in their wall

564
Q

Compromise between what tow factors? (cell wall)

A

A good enough cell wall that the plant can grow well and a cell wall thats easy to process

Reduced lignin = more susceptible to wind damage and not as strong and pathogen attack

565
Q

How do plant cells communicate

A

Plasmodesmata

  • plasma membrane is continuous between two cells
  • small enough to prevent organelle movements
  • allow the free exchange of small molecules.
566
Q

Pit field

A

Aggregation of plasmodesmata

567
Q

Properties of plasmodesmata

A
  • plasma membrane is continuous between two cells (goes through the gaps)
  • small enough to prevent organelle movements
  • allow the free exchange of small molecule (Eg Water)
568
Q

How are things stopped from being moved through plasmodesmata

A

They are quite small

569
Q

Example of substance that can cross plasmodesmata freely

570
Q

What is another structure apart from the plasma membrane that goes from one cell into the other

A

Endoplasmic reticiulum

571
Q

What are the two structures that go across from one cell into the other in plants

A
  • Plasma membrane

- Endoplasmic reticulum

572
Q

How do viruses take advantage of plasmodesmata

A

Alfalfa mosaic virus

  • too big to go through plasmodesmata

Two components of viruses: protein coat and nucleic acid

  • Leave coat in first cell, just move nucleic acid through plasmodesmata.
  • with aid of gating (movement) proteins
  • within genome, has a gene that encodes for the protein
573
Q

Special protein that helps move through plasmodesmata in virus

A

Gating (movement) proteins
- attaches to viral nucleic acid and helps it move into the plasmodesmata

enables virus to spread rapidly throughout the leaves

574
Q

Potato leafroll virus

A

Leaves roll up = reduced ps

575
Q

Genetic engineering for viral infections in plants

A

Introduced into plant genome a gene that encodes for the transport protein
- put a mutant -> non functional protein

  • mixed population of wild-type (work fine) and modified (mutant, non functional)
  • both associated with the nucleic acid
  • enough to stop the function of the proteins that do work
    = don’t get movement through plasmodesmata

= infection localised and doesn’t spread.

576
Q

What plastid does Proplastid develop in response to light

A

Chloroplast

577
Q

Chromoplasts

A
  • attract animals - give colour to many flowers and fruits

- increased carotenoids (pigments) and decreased thylakoid membranes (light reaction)

578
Q

What do chromoplasts contain

A

Increased carotenoids and decreased thylakoid membranes

579
Q

Conversion when a green tomato ripens

A

Chloroplasts in unripe break down and are converted to chromoplasts in ripe tomatoes

  • signal to animals that this fruit is palatable and ready
  • breakdown of chlorophyll, accumulation of carotenoids
580
Q

What are leucoplasts

A

Storage:

  • pigments
  • protein
  • lipids
  • starch

eg starch in leucoplasts in potato

NO highly differentiated thylakoid membrane

581
Q

Two types of photosynthesis

A

Oxygenic and an oxygenic

582
Q

Flow of biological energy

A

Light E -> organic molecules and O2 -> respiration -> CO2 + H2O

583
Q

Can food production match demands of a growing pop?

A

Predicted increase is smaller than the increase required to meet predicted demand (for maize, rice, wheat, soybean)

  • maybe improving photosynthesis would improve crop production
  • inc productivity
584
Q

Two stages of ps

A

Light reactions and Calvin Cycle

585
Q

Where does light reaction occur

A

Thylakoid membrane

  • photolysis of water
  • ATP and NADPH produced
586
Q

Where does Calvin Cycle occur

A

Stroma

  • carbon fixation
  • ADP and NADP+
587
Q

Maximising SA of plant

A
  • Maximise leave
  • chloroplast to outer edge of cells
  • thylakoid membranes
588
Q

How is light absorbed

A

by pigments

absorb photons

589
Q

3 pigments in chloroplast

A

Chl a
Chl b
carotenoids

590
Q

Which colour is the least absorbed

A
  • green (of all three pigments)

- modify pigments that could absorb extra wavelengths to inc productivity of photosynthesis

591
Q

Action spectrum

A

O2 evolution

  • dip in green = no O2 when do ps due to no light absorbed
592
Q

Engelmann’s expt

A

Took filament of algae
- use prism to divide light into diff wavelengths

  • put aerobic bacteria
    Aerobic bacteria does well where the algae is photosynthesising and producing O2
593
Q

Two primary pigments in ps

A

chl a and chl b

594
Q

How do chl a and chl b differ

A

CHO in chl b

CH3 in cola

595
Q

Structure of chlorophyll

A

Hydrophobic tail - interacts with protein.
- anchors molecule into light harvesting complex

  • porphyrin ring
  • harvest light energy
  • absorb photon
  • wavelength depends on group
  • Mg absorbs photon
596
Q

Which part of the chlorophyll interact with protein

A

Hydrophobic tail

597
Q

Which part of chlorophyll harvest light E

A

Porphyrin ring

598
Q

How does the chlorophyll sit in membrane

A

Complicated group on a stick that’s embedded in a protein in membrane.

599
Q

What are chlorophyll associated with

A

Photosystems

600
Q

Structure of photosystem

A

Light harvesting complexes around the reaction centre

- reaction centre in middle

601
Q

Process of light harvesting in photosystems

A
  1. Photon absorbed by chlorophyll molecule
  2. Light Energy from photo passes to chl. Transfer of E from one chl to another
    - continues until transfer of E to chl in the reaction centre.
    - chl in reaction center are called “special chl molecules”
    - they are not different but have different protein environment in rh reaction centre
  3. excitation of electron from special chl
    - E transfer from chl to special chl, excitation of electron
    - excited electrons leaves and transfers to another molecule -> primary electron acceptor = first molecule that takes the electron from the chl.
  • charge sep -> movt of high E electron.
  • light E -> CPE
602
Q

What is the reaction centre made of

A

Pigment-protein complex

603
Q

What happens to the electron released from chl

A

Move into the photosynthetic electron transport chain

604
Q

Process of ps ETC

A
  1. Both Photosystems II and I absorb light E
    - light go through light harvesting complex
    - both have special chl in reaction centers
    - excitation of electron and go to primary electron acceptor
    - electrons leave the photosystem
  2. electrons from PS II go to cytochrome complex (which doesn’t not absorb light E
    - act as channel
    - move through channel and go to PS I
    - replace two e- that left PS I
  3. movement of e- across thalloid membranes results in H+ pumping across thylakoid membrane from outside to inside.
  4. electrons that left PS I go to NADP+ reductase
    - make NADP+ + H+ -> NADPH
    - high E electrons in NADPH (E carrying molecule) (used in Carbon fixation)
  5. Replace lost electrons from PS II from photolysis of water
    - H2O -> 0.5O2 + 2H+ (Get two electrons)
    - energetically unfavourable
    - catalytic center allows two e- to be drawn from water.
    - O2 as byproduct (O2 is the terminal electron acceptor in respiration)
    - accumulation of H+ on inside
  6. H+ go through ATP synthase, flow down conc grad to outside of thylakoid into stroma.
    - ATP generated

ATP and NADPH go to Calvin Cycle

605
Q

Smaller complexes in membrane

A

Mobile electron carriers that can move through thylakoid membrane carrying those electrons.

606
Q

Compare and contrast high H+ conc in mt and ct

A

mt: intermembrane space
ct: thylakoid space

Important of organelles

both have ATP synthase
H+ flow through down conc grad.
- into stroma
- into matrix

607
Q

Overall, what happens in the light reactions

A
  • water split
  • O2 produced
  • ATP and NADPh produced
608
Q

Overall, what happens in the Calvin Cycle

A

ATP and NADPH produced in the light reactions are used to fix CO2 and produce carbohydrate
- in stroma

  • Fix 3CO2 into 1 high E 3C compound.
609
Q

3 steps of Calvin Cycle

A
  1. Carbon fixation
    - fix CO2 into carbohydrate
  2. Reduction
  3. Regeneration of CO2 acceptor
610
Q

Process of Calvin Cycle

A
  1. 3 x 5C
  2. 3 x CO2
  3. CARBON FIXATION uses Rubisco
  4. 6 x 3C
    - need 6 ATP -> 6ADP
    - need 6 NADPH -> 6NADP+ + 6Pi
  5. REDUCTION. Makes 1 x 3C compound
    - goes off to form glucose and other compounds
  6. left with 5 x 3C
  7. REGENERATION OF CO2 ACCEPTOR uses 3ATP
  8. Back to 3 x 5C
611
Q

Most abundant protein in plant

A

Rubisco (catalyses carbon fixation)

612
Q

eg potato on windowsill

A

Leucoplast convert to chloroplast in response to light stimulus
- production of thylakoid membranes

613
Q

What is

A

Undifferentiated organelle

  • harvest light E
  • convert into chemical E
614
Q

Describe chloroplast development triggered by light

A
  • Dispersion of prolamellar body within the primary layer of labelled
  • formation of grana after 24 hours of continuous light exposure
  • 48 hours later fully differentiated chloroplast
  • refer to diagram
615
Q

Two compounds of pigments in periwrinkles

A

Vinblastine and vincristine

- also anti-cancer

616
Q

Similarities between E generation in A and P cells

A

Sim:

  • ATP by chemiosmosis
  • ETC pump H+ across membrane from low to high conc
  • H+ diffsuse back in thru ATP synthase -> ATP synthesis
  • electron carriers are sim
  • ATO synthase are sim

Diff:

  • flow of H+
  • high energy electron from oxidation of organic molecules vs electron from H2O
  • transfer CPE to ATP vs transform light E to CPE in ATP
  • ATP production in matrix vs ATP produced in stroma
617
Q

Where are the high energy electrons from in mt and ct

A

in mt: from oxidation of organic molecules

- in ct: from water.

618
Q

Function of nucleolus

A

rRNA synthesised from DNA
- protein imported from cytoplasm are assembled with rRNA into large and small ribosomal subunits (these subunits then exit the nucleus through the nuclear pores to the cytoplasm, where a large and small subunit can assemble into a ribosome

619
Q

Things that go out of nuclear pore

A
  • rRNA
  • mRNA
  • tRNA
  • ribosomal subunits
620
Q

Things that go into the nucleus

A
  • control signals eg growth factors, hormones
  • E and materials eg ATP
  • proteins needed for transcription
  • protein needed for chromosome replication
  • ribosomal proteins
621
Q

Where are plastids found

A

actively dividing root and shoot tissue

622
Q

What do light reactions produce

A

NADPH, ATP, O2

623
Q

Function of plasmodesmata

A

Allow continuity of PM from 2 adjacent cells and cytoplasmic exchange between cells

624
Q

Structure of plasmodesmata

A

narrow cylindrical desmotubule derived from ER, surrounded by a narrow ring of cytoplasm (annulus)

625
Q

Which substances can cross plasmodesmata

A

H2O, glucose, even proteins and RNA

  • plant viruses
  • as viral RNA is too large to move freely through the channels, gating (movement) proteins bind to the viral nucleic acids and “thread” the RNA thru the plasmodesmata into an adjacent cell where replic take place
626
Q

How do viruses pass through plasmodesmata

A
  • as viral RNA is too large to move freely through the channels, gating (movement) proteins bind to the viral nucleic acids and “thread” the RNA thru the plasmodesmata into an adjacent cell where replic take place
627
Q

Chemical structure of lignin

A

Complex phenolic polymer