Topic 2 Flashcards

1
Q

Write the 4 groups found in an amino acid

A
  • H group
  • R group, residual group, side chain
  • Amine group, NH2
  • Carboxyl group, COOH
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2
Q

Name the bonds found in the primary structure of a protein

A

Peptide bonds

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3
Q

Are enzymes fibrous or globular prteins?

A

globular

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4
Q

Which bond can be found in both secondary an tertiary structure of proteins?

A

Hydrogen

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5
Q

Where in the cell are polypeptides made?

A

ribosomes

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6
Q

What is a conjugates protein?

A

A protein containing a non-protein molecule/chemical or a prosthetic molecule

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7
Q

State examples of a conjugated protein

A
  • Haemoglobin
  • Lipoprotein
  • Glycoproteins
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8
Q

Which 3 bonds can be found in the tertiary structure of a protein?

A
  • Disulphide links
  • Hydrogen bonds
  • Ionic bonds
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9
Q

State the structural similarities between fibrous and globular proteins

A
  • Both contain primary structures
  • Have hydrogen and peptide bonds
  • Both are a long polypeptide chain
  • Both made of amino acids
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10
Q

Is fibrin a fibrous or globular protein?

A

Fibrous

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11
Q

Are enzymes soluble or insoluble?

A

soluble

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12
Q

What is the difference between the amino acid R groups on the outside of a globular protein and the amino acid R groups on the outside of a fibrous protein?

A

A R group on the outside of a globular protein will be polar and therefore hydrophilic, meaning the protein is soluble. A R group on the outside of a fibrous protein with be non-polar and therefore hydrophobic, meaning the protein is insoluble. This is because globular proteins have tertiary structure whereas fibrous proteins don’t`

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13
Q

Which part of an amino acid is the variable group?

A

the R group

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14
Q

Between which 2 groups does a peptide form?

A

N-H2 and the C=O
H-N-C=O

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15
Q

Is haemoglobin a fibrous or globular protein?

A

Globular

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16
Q

What is the key property difference between fibrous and globular proteins?

A

Globular are soluble, Fibrous are insoluble

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17
Q

Between which type of R groups does an ionic bond form?

A

Delta positive charged and delta negative charged, polar R groups

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18
Q

Name the two types of secondary structure

A
  • alpha helix
  • beta pleated sheet
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19
Q

How many subunits are present in haemoglobin?

A

4

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20
Q

Collagen is described as a _______ helix

A

triple

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21
Q

Define primary structure of a protein

A

A specific sequence of amino acids joins together by peptide bonds (condensation) to form a polypeptide chain

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22
Q

A disulphide bond forms between two R groups which contain_______

A

sulphur
-SH
the amino acid cysteine

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23
Q

Name the four chemical elements that all amino acids contain

A
  • C, H, O, N
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24
Q

A protein with quaternary structure has more than one _______

A

polypeptide chain

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25
Q

Name proteins with a quaternary structure

A
  • collagen
  • haemoglobin
  • insulin
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26
Q

What does a polypeptide need to do to form a protein?

A

Fold, become structured, into a more 3D shape

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27
Q

Is collagen soluble in water?

A

no

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28
Q

What does the enzyme amylase have on its surface which makes it soluble?

A

Polar R groups (hydrophilic)

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29
Q

Which non-protein group does haemoglobin contain that makes it a conjugated protein?

A

Haem group

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30
Q

State the key properties of collagen which make it good for its function

A
  • Insoluble
  • Fibrous protein allows for length to vary to the collagen fibres can adapt to the right size for their placement
  • Lots of hydrogen bonds and strong peptide bonds make for high tensile strength
  • some flexibility
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31
Q

When 2 amino acids form a dipeptide, which type of reaction takes place?

A

condensation

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32
Q

Define ‘polypeptide’

A

A polymer made of many amino acids, joined by peptide bonds to form a long chain

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33
Q

If a polypeptide chain contains 150 amino acids, how many peptide bonds will it contain?

A

149

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34
Q

Draw a peptide bond

A

O-NC=O

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35
Q

If a polypeptide contains 195 amino acids, how many molecules of water will be needed to fully hydrolyse it into amino acids?

A

194

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36
Q

Where in a cell does a polypeptide fold to form a functional protein?

A

In the lumen of the endoplasmic reticulum

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37
Q

What structural feature does an enzyme have which other globular proteins do not?

A

active site

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38
Q

What shape are globular proteins?

A

Spherical

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39
Q

What is the function of glycoproteins?

A

act as receptors on cell membranes

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40
Q

What is the function of haemoglobin?

A

to bind oxygen to red blood cells for transportation

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41
Q

Fibrous proteins have a _________ sequence of amino acids

A

repetitive

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42
Q

What is keratin?

A

A fibrous protein found in hair, nails, horns

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43
Q

List examples of fibrous proteins

A
  • collagen
  • fibrin
  • keratin
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44
Q

Fibrous proteins have important _______ roles

A

structural

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45
Q

How are R groups positioned in a globular protein?

A

Polar groups on the outside, non-polar groups on the inside

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46
Q

Globular proteins have important roles in _____

A

metabolic reactions

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47
Q

List examples of globular proteins

A
  • Enzymes
  • Haemoglobin
  • Thrombin, Fibrinogen, prothrombin
  • insulin
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48
Q

Define tertiary structure

A

the further folding of the secondary structure into a precise/specific 3D shape

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49
Q

The primary structure determines _____________

A

the position of amino acid R groups

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50
Q

What is the monomer of proteins?

A

amino acids

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51
Q

Plants can make ___ amino acids and animals can make ______ amino acids

A
  • all
  • only some
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52
Q

What are essential amino acids?

A

the amino acids that animals must obtain from their diet

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53
Q

What id the dimer of amino acids called?

A

dipeptide

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54
Q

What holds together tertiary structures?

A

chemical bonds and hydrophobic interactions between R groups

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55
Q

What four types of R group are there?

A
  • Nonpolar
  • Polar
  • Electrically charged - negative, acidic
  • Electrically charged - positive, basic
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56
Q

How many different R groups are there and therefore the number of different amino acids?

A

20

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57
Q

State the function of cholesterol in the cell membrane

A

Cholesterol regulates the fluidity of the membrane

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58
Q

Which type of molecule forms the bilayer which is the cell membrane?

A

Phosopholipids

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59
Q

Is carbohydrate found on the inside or outside of the membrane?

A

outside

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60
Q

Describe the head of a phospholipid

A
  • Hydrophilic
  • Made of glycerol and a phosphate group
  • Attached to two fatty acid chains
  • Found on the surface of the bilayer
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61
Q

How many fatty acid tails are found in a phospholipid?

A

2

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62
Q

Where is cholesterol found in the cell membrane?

A

imbedded in the bilayer surface, in between the phospholipid tails

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63
Q

How many layers of phospholipids make up the cell membrane?

A

Two , therefore bilayer

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64
Q

What is the role of channel proteins in the cell membrane?

A

Facilitated diffusion -Channel proteins transport larger polar molecule through small water filled pathways

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65
Q

State 2 parts of the bilayer that water can pass through the bilayer.

A
  • proteins
  • phospholipids
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66
Q

State properties of cell membrane

A
  • Fluid
  • Flexible
  • Bilayer
  • Partially/selectively permeable
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67
Q

Which word described the fatty acid tails of a phospholipid and means ‘water hating’?

A

Hydrophobic

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68
Q

Give one function of a membrane glycolipid

A

Act as a receptor, cell to cell recognition

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69
Q

Which molecules bind to carbohydrate and were used to prove that carbohydrate was only found on one side of the cell membrane?

A

Lectins

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70
Q

Are channel proteins transmembrane proteins?

A

Yes

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71
Q

Which technique helped scientists prove that proteins were embedded in the cell membrane rather than attached to the outside of it?

A

Frozen fracture

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72
Q

Molecules attached to the cell membrane which contain active are called ________

A

Enzymes

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73
Q

What type of protein is the CFTR protein?

A

Mucus

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74
Q

Do channel proteins span the membrane or are they only found on one side?

A

Span the membrane

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75
Q

Describe the evidence which supported the idea that the cell membrane is a bilayer.

A

Red blood cell membranes were digested and the lipids spread on the surface of water. The surface area that they covered on water was twice the surface area of the surface area of the red blood cell. Therefore there must be a double layer of lipid around the cell.

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76
Q

Give the function of a glycoprotein

A

Acts as a receptor, cell to cell recognition

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77
Q

Which chemical element do phospholipids contain that triglycerides do not?

A

Phosphorus

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78
Q

Which part of a phospholipid is hydrophobic?

A

The fatty acid tails, hydrocarbon chains

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79
Q

Name the aqueous environment found on the inside of a cell membrane?

A

Cell cytoplasm

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80
Q

Name the aqueous environment found on the outside of a cell membrane?

A

Tissue fluid

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81
Q

Why do phospholipids spontaneously form a bilayer?

A
  • Most stable structure of phospholipids.
  • Phosphate heads of phospholipids are hydrophilic – so they attract and interact with water on the membrane surfaces (both sides) Fatty acid tails of phospholipids are hydrophobic - so they repel and orientate themselves away from water inside the membrane
  • Bilayer arrangement is due to the aqueous environment on both sides of the membrane (cytoplasm inside, tissue fluid outside)
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82
Q

What does ‘fluid mosaic’ mean in the term fluid mosaic model?

A

Fluid- ‘sea’ of phospholipids are able to move, fuse, pinch or change shape. Proteins are able to move
Mosaic- proteins interspersed through the bilayer, randomly scattered pattern

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83
Q

What are the differences between the ‘Davson-Danielli three layer sandwich’ model of the cell membrane and the present day ‘fluid mosaic’ model?

A
  • FMM - Phospholipid head are on the outside
  • FMM - Proteins are imbedded in the bilayer
  • TLS - no carbohydrates present
  • TLS - has no cholesterol
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84
Q

Describe the evidence which supports the idea that the cell membrane is fluid

A
  • The proteins from the human cell and the mouse cell were able mix and therefore the proteins must be able to move across the fluid membrane
  • Proteins in 2 different cells labelled with fluorescent markers each of a different colour, 2 cells are fused together, proteins intermix , so proteins must be able to move within the plane of the bilayer
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85
Q

Which monomers are the proteins found in the cell membrane made from?@

A

amino acids

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86
Q

State the function of a carrier protein

A

To move larger molecules through the bilayer via facilitated diffusion or active transport which requires ATP
- transport type depends on concentration gradient

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87
Q

What was the results of Davson and Danielli experiments?

A

In 1954, electron microscope images showed more detailed images of the cell membrane
- different layers could be seen in the cell membrane

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88
Q

What was the results of Gorter and Grendel experiments?

A

In 1924, red blood cell membranes contain enough phospholipids to cover the red blood cell twice
- Showed the cell membrane is a phospholipid bilayer

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89
Q

At first what were the dark outer layers and lighter inner layers thought to be?

A
  • inner layer thought to be lipid
  • outer layer thought to be protein
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90
Q

Explain the freeze fracture results

A

The freeze fracture showed ‘bumps’ in the centre of the membrane
- proteins are found embedded in the bilayer rather than either side

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91
Q

Explain the results of Frye and Edinin experiments

A

The proteins of two cells were labelled with different colour fluorescent markers and fused. The coloured markers intermixed
- the membrane is fluid which allows many proteins to move as the phospholipids move

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92
Q

What was the results of Unwin and Henderson experiments?

A

In 1984, some proteins can only be released from the cell membrane using strong detergents which dissolve the membrane. Others can be released more easily by increasing ionic strength
- found intrinsic proteins which are fully imbedded in the cell membrane and extrinsic proteins are loosely associated with the cell membrane

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93
Q

Explain the Lectins
results

A

Only bound to the outside of the cell membrane
- Carbohydrate is only found on the outside surface of the cell membrane

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94
Q

What are lectins?

A

Molecules which bind to carbohydrate

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95
Q

What are the 3 ways you can disrupt a cell membrane?

A
  • Detergents, grab onto lipids
  • extremes of temperature
  • alchohol
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96
Q

Membranes enable ____________

A

Compartmentalisation
- allows for a concentration gradient to be created across membranes

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97
Q

How wide is the bilayer?

A

7nm

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98
Q

What is a micelle?

A

Spherical clusters with hydrophobic tails pointing into the centre

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99
Q

What components are in the fluid mosaic model?

A
  • intrinsic/extrinsic proteins
  • glycolipid
  • glycoprotein
  • transmembrane proteins
    -channel proteins
    -carrier proteins
  • cholesterol
  • phospholipid bilayer
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100
Q

Who came up with the three-layer protein-lipid sandwich model?

A

Singer and Nicholson in 1972

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101
Q

By which transport process does carbon dioxide pass through the cell membrane?

A

Diffusion

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102
Q

Are carrier proteins involved in facilitated diffusion?

A

Yes

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103
Q

Which three transport processes require energy in the form of ATP?

A
  • endocytosis
  • exocytosis
  • active transport
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104
Q

Where exactly is the CFTR protein found in the body?

A

In the cell membrane of mucus producing cells in respiratory, digestive and reproductive systems

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105
Q

What does the CFTR protein transport?

A

Chloride ions

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106
Q

Through which two components of the cell membrane can water pass by osmosis?

A
  • through channel proteins (aquaporins)
  • Phospholipid bilayer
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107
Q

Define facilitated diffusion

A

the movement of molecules/ions from a region of high conc. to a region of low conc. down a concentration gradient through a channel/carrier protein in the membrane

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108
Q

Can lipid soluble molecules pass directly through a lipid bilayer?

A

yes

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109
Q

Compare simple diffusion to facilitated diffusion

A
  • Both are the movement of substance down a concentration gradient
  • Facilitated diffusion uses proteins and simple diffusion does not
  • Facilitated always takes place through a membrane, diffusion doesn’t always
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110
Q

State the key differences between active transport and facilitated diffusion

A
  • Active transport uses ATP, f. diffusion doesn’t
  • Active transport transports substances against the conc.
    gradient, f. diffusion goes down the conc. gradient
  • active transport is only one way, f. diffusion is both
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111
Q

Explain the process of exocytosis

A
  • this is the excretion of large molecules from a cell
  • a vesicle within the cell that is carrying a substance moves towards the surface cell membrane
  • the vesicle fuses to the cell membrane and then comes apart to release the molecules out of the cell
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112
Q

By which transport process would amino acids enter a cell, if there was a higher concentration of them outside the cell than inside?

A

Facilitated diffusion

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113
Q

Define osmosis

A

the net movement of free water molecules from a region of low solute conc. to a region of high solute conc. over a partially permeable membrane

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114
Q

Can ions pass directly through the lipid bilayer?

A

No as they are charged

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115
Q

Does facilitated diffusion require ATP?

A

No

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116
Q

Which type of proteins are involved in active transport?

A

specific carrier proteins

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117
Q

Describe how a white blood cell engulfs a bacterium

A

By endocytosis
- the cell membrane caves in to form a pocket around the bacterium (encloses the bacterium)
- the membrane comes back together and pinches off so the a vesicle is formed inside of the cell

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118
Q

Define active transport

A

the movement of molecules/ions against a conc. gradient by using carrier proteins and ATP

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119
Q

Compare osmosis and active transport

A
  • Osmosis only moves water molecules
  • Both transport molecule through a membrane
  • active transport is against the conc. gradient, osmosis is down the conc. gradient
  • Active transport requires ATP and carrier proteins
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120
Q

By which process does oxygen pass through the cell membrane?

A

simple diffusion

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121
Q

When equilibrium has been reached across a membrane, do the molecules stop moving?

A

No however there is no overall net movement, at the same rate

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122
Q

What does ‘no net movement mean’?

A

The molecules are still moving but there isn’t a favoured direction (conc. stays the same on both sides of the membrane) move at the same rate

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123
Q

When there is a large concentration difference between the inside and outside of a cell, does this lead to a fast or slow rate of diffusion

A

fast rate of diffusion

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124
Q

If a molecule is in high concentration outside a cell but does not enter a cell, what does this tell you about the permeability of the membrane to that molecule?

A

The membrane is impermeable to the molecule

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125
Q

Why can starch not diffuse out of plant cells, but glucose can?

A

Starch is too large a molecule to diffuse in between the cell membrane bilayer (also insoluble)

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126
Q

If water moves from an area of high concentration of free water in the air space of a leaf, through a stoma (pore) to an area of low free water outside the leaf (in the air), why is this not osmosis?

A

Because osmosis is over a partially permeable membrane. there was no membrane in this case so it was diffusion

127
Q

What happens when the uptake of glucose into a cell as the concentration gradient becomes less steep?

A

glucose uptake slows down

128
Q

Compare the processes of endocytosis and exocytosis

A
  • Endocytosis is movement into a cell whereas exocytosis is movement out of a cell
  • Both use vesicles and the cell membranes fluidity to move large (volumes of) substances
  • both involved in bulk transport
  • both require energy
  • both involve membranes fusing
129
Q

What do high ethanol concentrations do to phospholipids?

A

Dissolves the phospholipid

130
Q

What do high temperatures do to membrane proteins?

A

Denature them

131
Q

If there are 40 glucose molecules in a cell at the start of an experiment and there are 65 glucose molecules in the cell at the end of the experiment, calculate the percentage increase in glucose molecules in the cell over the course of the experiment

A

25/40= 0.625
x 100= 62.5%

132
Q

What type of protein is the CFTR protein?

A

channel protein

133
Q

What are the active transport processes?

A
  • active transport
  • exocytosis
    -endocytosis
134
Q

What are the passive transport processes?

A
  • diffusion
  • facilitated diffusion
  • osmosis
135
Q

What is a partially permeable membrane?

A

a barrier to some solutes but not water

136
Q

What type of molecule does diffusion transport?

A
  • non-polar, uncharged, lipid soluble, hydrophobic, small molecules
137
Q

What type of molecule does facilitated diffusion transport?

A

charged, ions, hydrophilic, larger than CO2

138
Q

What is ATP?

A

An energy transfer molecule used for all biological processes as an immediate source of energy#
- adenosine triphosphate

139
Q

What are active transport proteins also known as?

A

( protein) Pumps

140
Q

Name the sugar found in DNA

A

deoxyribose

141
Q

State the name of the base which pairs with thymine in DNA

142
Q

Which type of bond holds the two strands together in DNA?

A

hydrogen bond

143
Q

State three parts of an RNA nucleotide

A
  • pentose sugar (ribose)
  • phosphate group
  • organic base e.g. adenine, cytosine, guanine and uracil
144
Q

Why is DNA replication described as semi-conservative?

A

In replication one strand of the DNA molecule will come from the original DNA double helix molecule and the other strand will have been newly formed from free mononucleotides

145
Q

Which organic base is found in RNA but not DNA?

A

uracil in the place of thymine

146
Q

Name the enzyme which joins mononucleotides in DNA replication

A

DNA polymerase

147
Q

Name the sugar found in RNA

148
Q

What is the function of DNA helicase in DNA replication?

A

to unwind, unzip, separate the 2 DNA strands

149
Q

Is RNA single or double stranded?

A

single stranded

150
Q

What is bonded to the pentose sugar in the DNA backbone?

A

A phosphate group

151
Q

If 24% of the bases in a DNA molecule are adenine, what percentage of the bases will be cytosine?

152
Q

How many template strands are there in DNA replication?

153
Q

Which base joins with cytosine in DNA?

154
Q

Which organic base is found in DNA but not RNA?

155
Q

Ina mononucleotide, is the base bonded to sugar or phosphate?

156
Q

If 68% of the bases in a DNA molecule are adenine, what percentage of the bases will be uracil?

A

0% as uracil is not present in DNA molecules

157
Q

Describe complementary base pairing in DNA

A

Each base in DNA has a specific base which it can pair up to
Cytosine - guanine (3 hydrogen bonds)
adenine - thymine (2 hydrogen bonds)
this is because A and C both have a two ring structure whereas G and T have a one ring. this means that each ‘rung’ is equal in the DNA so it is a uniform width

158
Q

Give the structural differences between DNA and RNA

A
  • DNA has thymine while RNA has uracil instead
  • DNA is double stranded whereas RNA is single stranded
  • DNA has the deoxyribose pentose sugar whereas RNA has the ribose pentose sugar
159
Q

Why is DNA described as a double helix?

A

this is because each DNA strand twists into a helical shape and as there are two strand the helix is double
made of two strand wound together

160
Q

Is DNA helicase an extracellular or intracellular enzyme?

A

intracellular

161
Q

Is RNA a polynucleotide? Explain

A

Yes as RNA is made of many RNA mononucleotides joined together by phosphodiester bonds

162
Q

Name the type of bond which joins mononucleotides in DNA

A

phosphodiester bonds

163
Q

Name the type of reaction which takes place when DNA is broken down into mononucleotides

A

hydrolysis

164
Q

Where in a cell does DNA replication take place?

165
Q

If there were 200 bases in an RNA molecule, how many water molecules would be needed to completely break the molecule down into mononucleotides?

166
Q

Name two nucleic acids

A
  • deoxyribonucleic acid, DNA
  • ribonucleic acid, RNA
167
Q

Is DNA polymerase an extracellular or intracellular enzyme?

A

intracellular

168
Q

In ‘heavy’ DNA, which isotope of nitrogen is present?

169
Q

Which part of a mononucleotide contains nitrogen?

A

organic base

170
Q

In ‘light’ DNA, which isotope of nitrogen is present?

171
Q

If a DNA molecule consists of one strand made of 14N and one strand made of 15N, where in a tube will the band of DNA form, when centrifuged in a density gradient?

172
Q

In Meselson and Stahl’s experiment, where did the band/s actually appear in the tube after the first round of semi-conservative replication?

A

the middle

173
Q

In Meselson and Stahl’s experiment, where did the band/s actually appear in the tube after two rounds of semi-conservative replication?

A

the middle and top

174
Q

If one DNA molecule went through 5 rounds of semi-conservative replication, how many DNA molecules would be produced?

175
Q

How many different RNA mononucleotides exist?

176
Q

Name the 2 types/theories of how DNA replication takes place that were refuted by Meselson and Stahl’s experiments.

A
  • Fragmentary (dispersive)
  • conservative
177
Q

What dictates the unique characteristics of an organism?

A

their genetic code

178
Q

Define gene

A

A sequence of bases on a DNA molecule that codes for a specific sequence of amino acids in a polypeptide chain

179
Q

What is the genome?

A

all the genes in an individual

180
Q

What are purines?

A

Organic bases with a two ring structure

181
Q

What are pyrimidines?

A

organic bases with a one ring structure

182
Q

What is the function of DNA ligase?

A

acts as an enzyme to help close any gaps in the strand that don’t have phosphodiester bonds

183
Q

Who carried out the experiment containing light and heavy strand of DNA?

A

Meselson and Stahl

184
Q

What bacterium did Meselson and Stahl use?

A

Escherichia coli, E.Coli

185
Q

What is the conservative replication theory?

A

one DNA molecule has two original strands and one molecule has two ‘new’ strands

186
Q

What is the fragmentary replication theory?

A

all DNA strands are made of a mixture of light and heavy DNA/ original nucleotides on new nucleotides

AKA dispersive replication

187
Q

How did Meselson and Stahl separate the DNA?

A

using centrifugation, a centrifuge

188
Q

How did Meselson and Stahl extract the DNA?

A

extracted the DNA from the bacteria using detergents

189
Q

Name the product of transcription

A

mRNA (messenger RNA)

190
Q

Which organic base is never found in mRNA?

191
Q

Where in a cell does transcription take place?

192
Q

Which DNA strand, sense or antisense, is the template for making mRNA?

193
Q

Name the enzyme which is needed for transcription

A

RNA Polymerase

194
Q

Does the whole DNA molecule unwind during transcription?

A

No, only the gene being transcribed

195
Q

Name the sugar found in mRNA

196
Q

Is mRNA single or double stranded?

197
Q

Why is the genetic code described as degenerate?

A

A amino acid can be coded for by several triplet codes

198
Q

If 499 mononucleotides are present in a molecule of mRNA, how many phosphodiester bonds will be present in the polynucleotide chain?

199
Q

24% of the bases in a mRNA molecule are adenine, 35% are cytosine and 12% are guanine. What percentage of the bases in the mRNA molecule are thymine?

200
Q

How many template strands are there in transcription?

201
Q

Which reaction joins the RNA mononucleotides in transcription?

A

Condensation

202
Q

48% of the bases in a mRNA molecule are adenine, 32% are cytosine and 10% are guanine. What percentage of the bases in the mRNA molecule are uracil?

203
Q

If these three triplets of bases are found on the DNA antisense strand, which bases will be transcribed into the molecule of mRNA?

  TTA   CAG   AGT
A

AAU GUC UCA

204
Q

What is the role of RNA polymerase in transcription?

A

Creates phosphodiester bonds between the mononucluotides

205
Q

What is the role of the antisense DNA strand in transcription?

A

To act as a template in which mRNA is built

206
Q

Why is the genetic code described as ˋtripletˋ?

A

Every three bases will code for one amino acid

207
Q

Describe the shape of a tRNA molecule

A

clover leaf shaped

Has an amino acid bonding site on one side and a specific anticodon the the bother side

208
Q

Where in the cell does translation take place?

A

Cytoplasm at ribosome

209
Q

Name the 4 key organelles/molecules that must be present for translation to take place

A
  • ribosome (top and bottom)
  • tRNA
  • mRNA
  • mononucleotides
210
Q

If a tRNA molecule was hydrolysed, name the monomers that would be released

A

Mononucleotides

211
Q

On which molecule would you find codons?

212
Q

On which molecule would you find anticodons?

213
Q

Name the type of bond that forms between a base in a codon and the complementary base of an anticodon

A

Hydrogen bond

214
Q

How many bases does one codon consist of?

215
Q

Name the type of bond that joins the amino acids in translation

216
Q

What is the product of translation?

A

Polypeptide chain

217
Q

What does the ribosome need to attach to before translation can start?

A

The mRNA molecule

218
Q

If there are 200 codons in a molecule of mRNA, how many amino acids is the polypeptide chain made from the mRNA likely to be made of?

219
Q

In the process of translation what is carried by a tRNA molecule?

A

One specific Amino acid

220
Q

What does the anticodon bind to?

A

The codon on the mRNA

221
Q

What is determined by the sequence on codons on a mRNA molecule?

A

The sequence of amino acids in a polypeptide chain

222
Q

Which cell organelle is made of rRNA?

223
Q

How many bases are present in 70 mRNA codons?

224
Q

What happens when a ribosome reaches a stop codon on a mRNA?

A

Can’t bind any new amino acid as there is no complementary tRNA so polypeptide chain is released

It detaches from the mRNA

225
Q

Where is the cell are ribosomes found?

A

Attached to the endoplasmic reticulum
Forming rough ER

226
Q

Define a gene

A

A section of organic bases in a specific sequence of DNA that codes for a specific sequence of amino acids in a polypeptide chain for a protein

227
Q

Which molecule in the cell contains the genetic code?

228
Q

Where does the polypeptide chain formed on the ribosome fold into a protein?

A

The lumen of the endoplasmic reticulum

229
Q

Compare DNA replication with transcription

A
  • Replication copies both DNA strands, transcription copies only one/antisense strand
  • Replication makes double stranded DNA, transcription makes single stranded mRNA
  • Replication uses the enzyme DNA polymerase, transcription uses RNA polymerase
  • Replication uses the base thymine/mononucleotide containing thymine, transcription uses uracil/ mononucleotide containing uracil
230
Q

What is the start codon?

A

AUG - methionine

231
Q

What is a stop codon also known as?

A

A chain terminator

232
Q

Define activation energy

A

The energy needed a reaction to occur
By causing bonds to {break / weaken / form}
Reduced by enzymes

233
Q

Are enzymes fibrous or globular proteins?

234
Q

Name two extracellular enzymes which are involved in blood clotting

A
  • thromboplastin
  • thrombin
235
Q

What is special about the active site, which makes it specific for a particular substrate?

A

The shape is specific/complementary to only one substrate. Lock and key model

236
Q

Give one difference between extracellular and intracellular enzymes

A

Extra cellular enzymes are found and function outside the cell whereas intracellular enzymes are catalyse reactions inside the cell

237
Q

Define biological catalyst

A

A catalyst made by an organism to lower the activation energy of reactions within the organism and to speed up the rate of reactions in the organism.

238
Q

Name the 2 key environmental conditions that affect enzymes

A
  • temperature
  • pH
239
Q

What forms as a transition state between the enzyme and substrate at the start of a reaction and the product/s at the end of a reaction?

A

Enzyme-substrate complex

240
Q

Do enzymes increase or decrease the activation energy for a reaction?

241
Q

What is similar about an active site and the substrate which fits into it?

A

They have the same shape/ a complementary shape

242
Q

Name an intracellular enzyme which is involved in DNA replication

A

DNA polymerase, DNA helicase

243
Q

What happens to an enzyme when it binds substrate in the induced fit theory?

A

The active site of the enzyme changes shape to conform around the shape of the substrate

244
Q

What is meant by enzyme specificity?

A

A enzyme is specific to a single substrate with an active site specifically shaped to bind and accept that substrate
-Enzyme has an active site with a specific shape which fits and binds to the complementary shape of the substrate – lock and key hypothesis to form enzyme-substrate complex, so each enzyme is specific for only one substrate

245
Q

What happens to pancreatic enzymes in a person with cystic fibrosis?

A

The are blocked by mucus in the pancreatic duct, they damage the pancreas and then are eventually broken down/destroyed

246
Q

Is thrombin an extracellular or intracellular enzyme?

A

extracellular

247
Q

Where are enzymes made in a cell?

A

ribosomes and fold in lumen of the endoplasmic reticulum

248
Q

Name the transport process which moves a large quantity of enzymes out of a cell

A

exocytosis

249
Q

Why would someone with cystic fibrosis be likely to have damaged insulin producing cells?

A

The digestive enzymes that are stuck in the pancreatic duct start to break down the pancreatic tissue which could result in the insulin producing cells being damaged

250
Q

How would amylase lower the activation energy for the breakdown of starch into glucose?

A

by providing an alternate reaction route

  • The way the substrate fits into the active site may put strain on some bonds so substrate distorted + bonds can be broken more easily
  • Active sites can have acidic amino acids which provide an acidic environment or basic amino acids which form an alkaline environment – each of these may be favourable for a specific reaction
251
Q

Name the substrate for the enzyme lipase

A

fats/trigylceride

252
Q

Is DNA helicase an extracellular or intracellular enzyme?

A

intrcellular

253
Q

How would you control the pH in an enzyme catalysed reaction?

A

Buffer solution

254
Q

What is an enzyme-substrate complex?

A

the intermediate stage where the substrate has been bound the the enzymes active site. Where bonds are broken/made. activation energy is lowered

255
Q

How would you control temperature in an enzyme catalysed reaction?

A

water bath

256
Q

Name the 2 products formed when the enzyme lipase breaks down a triglyceride

A
  • 3 fatty acids
  • glycerol
257
Q

Name the 2 products formed when the enzyme lactase breaks down the disaccharide lactose

A
  • glucose
  • galactose
258
Q

Describe an active site

A
  • specific to the shape of the substrate
  • may change shape the mould around the substrate
  • is where the substrate binds to an enzyme to be broken down/built up
  • small depression with a specific shape to fit the substrate
259
Q

When enzymes are exposed to temperatures above their optimum, what happens to them?

A

their active site starts to denature, resulting in them eventually becoming inactive

260
Q

Why does the rate of a reaction increase as temperature increases?

A

The kinetic energy increases so there are more frequent substrate-active site collisions. this means more enzyme-substrate complexes meaning more product formed in given time

261
Q

Why does the rate of an enzyme catalysed reaction decrease over time if a fixed volume of substrate is added at the start and no further substrate is added during the reaction?

A

Substrate eventually runs out as it is used up in the reaction

262
Q

What makes an enzyme soluble in water?

A

the many polar r-groups on the outside of the protein

263
Q

Which bonds may be present in the tertiary structure of an enzyme?

A
  • hydrogen
  • ionic
  • disulphide
264
Q

What happens to the rate of an enzyme catalysed reaction, as the enzyme concentration increases (assuming there is excess substrate)?

A

the rate of reaction increases proportionally

265
Q

How would you measure the rate of an enzyme catalysed reaction if one of the products is a gas?

A

By collecting the gas in a gas syringe/measuring cylinder

266
Q

Which part of an enzyme makes it specific for a particular substrate?

A

its active site

267
Q

What is the difference between a biological catalyst and a chemical catalyst?

A

a biological catalyst is made by the organism to be used to speed up reactions in the organism, chemical catalyst is not

268
Q

Where would you find hydrophobic amino acids in and enzyme?

A

On the inside/centre

269
Q

Which parts of amino acids are joined by bonds in the enzyme tertiary structure?

A

the r-groups

270
Q

What are the main types of mutation?

A
  • point mutation (substitution)
  • deletion
  • duplication (insertion)
  • inversion
271
Q

What is a germ line mutation?

A

Occurs in the DNA of an ovary or testis cell that is dividing to form an egg or sperm
- passed on to future generations
- present in every cell

272
Q

What is a somatic mutation?

A

A mutation that happens in all cells but gametes
- will die with the individual
- happens after conception

273
Q

What is the process when the mucus is too watery?

A
  • Na ions are actively pumped across the basal membrane
  • Na diffuses through sodium channels in the apical membrane
  • Cl diffuses down electrical (electrochemical) gradient through the gap junction
  • water is drawn out of cells due to high solute concentration in tissue fluid
  • water is drawn out of the mucus into the epithelial cell by osmosis
274
Q

What is the process when the mucus is too sticky?

A
  • Cl ions are transported via facilitated diffusion across the basal membrane
  • Cl ions diffuse through open CFTR channels
  • Na ions diffuse down the electrochemical gradient through the gap junction into the mucus
  • high solute concentration in mucus draws water out of epithelial cells
  • water is drawn j to the cell from tissue fluid by osmosis
275
Q

What happens to the mucus if the CFTR is missing/non-functional?

A

Cl ions are pumped into the cell so solute increases. Na ions are continuously pumped out of the mucus through the permanently open Na channel. Water is continuously removed from the mucus by osmosis

276
Q

What happens as a result of a mutation?

A

A change in the base sequence of DNA leads to different triplet/codon created leads to different R-group, different folding, different 3D specific shape. Leads to no function, no/faulty protein

277
Q

What systems does CF effect?

A

Respiratory, digestive, reproductive

278
Q

What is ficks law?

A

Rate of diffusion= (surface area X difference in conc)/thickness of gas exchange surface

279
Q

How does CF cause problems in the lungs?

A

The sticky mucus is too difficult for cilia to move so the trapped pathogens stay. Increasing risk of infection. The extra mucus also increases the diffusion distance. The mucus can also cause blockages which reduces surface area

280
Q

What problems does CF have on the digestive system?

A

The pancreatic duct becomes blocked by the sticky mucus, reducing digestive enzymes. This can lead to malabsorption syndrome. The pancreatic tissue can become damaged and insulin producing tissue due to the build up of enzymes leading to hard fibrous cysts

281
Q

What is the effect or CF on the reproductive system?

A

Female: a mucus plug will develop in the cervix, impairing fertilisation rates
Male: vas deferens can be missing or can be blocked by mucus impairing the release of sperm

282
Q

How are the lungs adapted for gas exchange?

A
  • large surface area- lots of alveoli
  • short diffusion distance- capillary and alveoli walls are thin
  • steep concentration gradient maintained by ventilation and circulation
283
Q

Enzymes are also known as…

A

biological catalysts

284
Q

What is a catabolic enzyme?

A

An enzyme that breaks down large molecules into smaller units

285
Q

What is an anabolic enzyme?

A

An enzyme that builds up substrates into a larger molecule

286
Q

What is an isomerase enzyme?

A

An enzyme that does not build up or break down the substrate is simply altered

287
Q

What is the initial rate of reaction?

A

the first rapid phase of the reaction that is used for comparison across enzyme controlled reactions

288
Q

What is the saturation point?

A

The point where there is a limiting factor

289
Q

What is the definition of a gene?

A

a sequence of bases on a DNA molecule that codes for a sequence of amino acid in a polypeptide chain

290
Q

Define locus

A

the position of a particular gene pair on each of the chromosomes

291
Q

Define homologous chromosomes

A

the chromosomes in a chromosomal pair

292
Q

define allele

A

An alternative form of the same gene
found at the same locus on a chromosome

293
Q

What is a genotype?

A

The combination of all alleles for one gene of the person

294
Q

What are homozygous genotypes?

A

When both alleles are dominant/recessive

295
Q

What are heterozygous genotypes?

A

When one allele is dominant and one is recessive

296
Q

What is a phenotype?

A

The genotype that is expressed (the characteristic)

297
Q

What is a dominant allele?

A

The allele that is always expressed
Will effect the phenotype of heterozygotes AND homozygotes

298
Q

What is a recessive allele?

A

The allele that will only effect the phenotype of a homozygote

299
Q

Carriers of CF have protection against what?

300
Q

Define monohybrid inheritance

A

The inherited characteristic is controlled by only one gene

301
Q

Define incomplete dominance

A

When neither allele is dominant and heterozygotes have an intermediate phenotype
- both alleles have an equal weighting in the expression

302
Q

Define genetic testing

A

Identifying the abnormal allele of the gene in the DNA of any cells

303
Q

Define genetic screening

A

Confirming the results of conventional tests to identify carriers and also to diagnose mutation in an embryo/foetus

304
Q

What are the possible sources used for genetic testing?

A
  • cheek cells and white blood cells from parents
  • cells directly from a foetus or embryo
305
Q

What are the 3 ways to test an embryo?

A

-Amniocentesis
- Chorionic villus sampling
- Non-Invasive prenatal Diagnosis (NIPD)

306
Q

What is Amniocentesis?

A

Procedure: a needle is inserted into amniotic fluid to collect foetal cells that have fallen of the placenta or foetus
Time Frame:15-17 weeks
Risk: 1%

307
Q

What is Chorionic villus sampling?

A

Procedure: small sample of placental tissue is removed, through wall of abdomen or vagina
Time Frame: 8-12 weeks
Risk: 1-2%

308
Q

What is NIPD?

A

Procedure: analyses DNA fragments in the mothers blood plasma during pregnancy
Time Frame: 7-9 weeks
Risk: None

309
Q

What is PGD?

A

testing before implantation
happens when there is a family history of a serious genetic condition
Procedure: couple undergo IVF so that embryo can be tested before transfer to the uterus- an early embryo can have a cell removed without causing harm

310
Q

What is autonomy

A

the idea that people can make up there own minds about things but have a duty to take into account how their actions might affect others

311
Q

Define co-dominance

A

When neither allele is dominant so BOTH phenotypes are FULLY expressed

312
Q

How many separate strands of DNA are there?

313
Q

What happens after cells for genetic testing have been collected?

A

The DNA is extracted and analysed to detects defective gene mutation