LS 2 midterm 1 Flashcards

1
Q

covalent bonds

A

two atoms share one, two, or three electrons –> very stable bond
most common

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2
Q

ionic bonds

A

either give up or accept electron from another atom to achieve a filled outer shell

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3
Q

hydrogen bonds

A

the attraction of the positive (hydrogen) end of the polar molecule to the negative end of another polar molecule (H - N,O,F) (high electronegativity)

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4
Q

van der waals forces

A

weak interactions between atos due to movement of negatively charged electrons resulting in formation of dipoles – transient, but in large quantities can cause significant changes

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5
Q

5 properties of water

A
  1. solvent - carries nutrients into body and wastes out; oxygen and CO2 can dissolve
  2. participates in chemical reactions - e.g. digestion
  3. absorbs and releases heat slowly - maintain homeostasis
  4. requires a large amount of heat to evaporate - perspiration can assist cooling of body
  5. provides lubrication - saliva, mucus because of cohesion and adhesion
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6
Q

inorganic compounds

A

water, inorganic acids, bases, and salts

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7
Q

organic compounds

A

carbs, lipids, proteins, nucleic acids

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8
Q

property of inorganic acids, bases and salts

A

all undergo ionization (dissociation) when dissolved in water in the body

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9
Q

how do acids ionize

A

produce hydrogen ions (protons) H+

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10
Q

how do bases ionize?

A

release hydroxyl ions (OH-)

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11
Q

how do salts ionize

A

cations and anions

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12
Q

what is a cation

A

positive ion

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13
Q

what is an anion

A

negative ion

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14
Q

importance of inorganic salts in body

A

components of cells and body fluid – sodium and chloride ions in extracellular fluid and potassium and phosphate ions inside cells

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15
Q

calculate pH

A

-logbase10[H+]

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16
Q

what pH represents neutral

A

7

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17
Q

what pH represent acidic

A

below 7 (1-7)

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18
Q

what pH represents basic

A

above 7 (7-14)

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19
Q

how does the body maintain constant pH (homeostasis)?

A

buffer systems

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20
Q

what is a buffer

A

a solution of a weak acid or weak base which remove excess H+ ions and OH- ions

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21
Q

pH of blood

A

7.35-7.45

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22
Q

pH of gastric juice (stomach)

A

1.2-3.0

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23
Q

types of lipids (4)

A
  1. fats (triglycerides)
  2. phospholipids
  3. prostaglandins
  4. steroids
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24
Q

what are fats and their purpose

A

(triglycerides) consist of one glycerol and 3 fatty acids; serve as a source of energy, and protect and insulate

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25
Q

unsaturated fat

A

fatty acids have a double bond

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26
Q

saturated fat

A

fatty acids are all single bonds

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27
Q

difference between fat and oil

A

fat is solid at room temp and oil is liquid

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28
Q

what are phospholipids

A

components of cell (plasma) membrane – lipid bilayer - polar head outside and nonpolar tail inside

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29
Q

what is amphipathic and example

A

polar and nonpolar parts - e.g. phospholipids

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30
Q

4 types of phospholipid movement

A
  1. rotational (rapid)
  2. diffusion (rapid)
  3. flexion (rapid)
  4. flip flop (rare)
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31
Q

rotational phospholipid movement

A

rotates along axis like a globe

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32
Q

diffusion phospholipid movement

A

lateral movement across bilayer (moves to diff spot in line)

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33
Q

flexion phospholipid movement

A

tails flex side to side

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34
Q

flip flop phospholipid movement

A

movement across bilayer, requires a special protein (moves to other side of bilayer)

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35
Q

what are prostaglandins

A

derivatives of fatty acids similar to hormones

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36
Q

what are fatty acids

A

chain of carbon atoms with a carboxyl group at one end

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37
Q

what are steroids

A

cholesterol is most abundant steroid in body and a component of cell membranes and steroid hormones are derived from cholesterol - ring structure

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38
Q

3 functions of carbohydrates

A
  1. provide energy
  2. form part of structural elements of some cells
  3. supply carbon atoms for synthesis of cellular components
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39
Q

what is glycogen

A

carb - stored form of glucose in liver and skeletal muscles for rapid needs
a polysaccharide that is the man energy source for animals
releases branched polymer of glucose

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40
Q

types of carbs

A

monosaccharides, disacharides, oligosacharides, polysacharides

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41
Q

molar ratio of carbs

A

C:H:O 1:2:1

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42
Q

how does the H:O ratio in carbs compare to lipids

A

much lower

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43
Q

what are monosaccharides

A

simple sugars - one molecules

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44
Q

3 main types of monosaccharides

A

glucose, fructose, galactose

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45
Q

what are disaccharides

A

2 monosaccharides bonded

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46
Q

3 main types of disaccharides & how they’re formed

A

sucrose, lactose, maltose (condensation reaction –> glycosidic reaction forms covalent bonds)

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47
Q

components of sucrose

A

glucose + fructose

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48
Q

components of lactose

A

glucose + galactose

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49
Q

components of maltose

A

glucose + glucose

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50
Q

what carb is milk sugar

A

lactose

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51
Q

what causes lactose intolerance

A

lack of enzyme lactase which breaks down lactose

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52
Q

what is an oligosaccharide

A

3-20 residues (sugars)

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53
Q

what is a polysaccharide and how can it be broken down

A

many monosaccharides bonded together (20+); broken down into constituent sugars by hydrolysis

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54
Q

what is cellulose

A

provides structural support to plants; unbranched polymer of glucose
layers of glucose that have H bond interactions

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55
Q

why is cellulose so strong

A

bc they lay flat and form h bonds between the layers

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56
Q

what are proteins and how are they linked

A

large complex molecules made up of amino acids, linked in sequence by covalent peptide bonds

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57
Q

what do amino acids consist of?

A

an amino group, carboxyl group, and a side chain

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58
Q

what is an amino group and it’s pH

A

-NH2; basic

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59
Q

what is a carboxyl group and it’s pH

A

-COOH; acidic

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60
Q

what is a side chain

A

the r group; different for each of the 20 different amino acids

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61
Q

5 roles of proteins

A
  1. cytoskeleton - supports and organizes cell components
  2. enzymes
  3. transport and storage of small molecules
  4. transmit info (hormones)
  5. defend against infection (antibodies)
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62
Q

what percent of enzymes are proteins

A

only 95%

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63
Q

what is primary structure of proteins

A

the amino acid sequence

- depends on specific amino acid at points along the chain and the number of amino acids making up the chain

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64
Q

what is secondary structure

A

local interactions
interactions between backbone
2 types:
alpha helices: corkscrew held together by hydrogen bonds
beta pleated sheets: protein chain loops back on itself (u-shape) like silk

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65
Q

tertiary structure

A

the 3d structure/conformation of the protein molecule, resulting from side chain interactions between different parts of the primary structure , all 4 types of bonds are possible e.g. hydrogen bonds, disulfide bridges between cysteine residues

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66
Q

quaternary structure

A

overall structure in a protein made up of more than one polypeptide chain (not all proteins have this)
interactions between multiple subunits of a protein

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67
Q

what structure is cholesterol

A

steroid ring structure

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68
Q

cholesterol is plants and animals?

A

absent from plasma membranes of most places, but present in up to 25% of lipid weight in plasma membranes of animals

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69
Q

do people need to consume cholesterol

A

no! body makes all cholesterol it needs in the liver

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70
Q

why is cholesterol needed

A

stabilizes the plasma membrane and helps produce bile salts for digestion

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71
Q

what happens if there’s too much cholesterol

A

can lead to deposition of excess in the walls of arteries (leads to athlerosclerosis)

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72
Q

why is LDL cholesterol “bad”

A

carries cholesterol to the tissues for use by cells

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73
Q

why is HDL cholesterol “good”

A

carries the cholesterol back to liver for excretion

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74
Q

proteins involved in muscle movement

A

actin and myosin (myosin head group pulls actin globules)

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75
Q

what does it mean to denaturize a protein

A

unfold the protein until it randomizes

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76
Q

what are nucleic acids

A

long polymers made up of nucleotides

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77
Q

chemical difference between RNA and DNA

A

H is in DNA and OH is in RNA

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78
Q

sugar components of nucleotides

A

deoxyribose is in DNA and ribose is in DNA

5’-3’ and 3’-5’

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79
Q

2 types of bases in nucleotides

A

purines and pyrimidines

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80
Q

purines

A

adenine, guanine

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81
Q

pyrimidines

A

cytosin, thyamine

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82
Q

complementary base pairs

A

adenine-thyamine and cytosine-guanine

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83
Q

3 types of RNA

A
messenger RNA (mRNA)
transfer RNA (tRNA)
ribosomal RNA (rRNA)
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84
Q

where does protein synthesis occur?

A

ribosomes

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85
Q

what is ribozyme

A

catalytic RNA, catalyst for making peptide bond between amino acids during protein synthesis

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86
Q

miller and Urey

A

synthesis of prebiotic molecules in an experimental atmosphere

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87
Q

types of tissue

A

epithelial tissue, coonective tissue, nervous tissue, muscle tissue

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88
Q

epithelial tissue

A

forms boundaries between parts of the body and has tight junctions keeping it sealed

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89
Q

connective tissue

A

cells in some sort of extracellular matrix

e.g. bone in a calcified matrix, blood cells in plasma, adipose cell in triglycerous matrix

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90
Q

nervous tissue

A

neurons conduct and generate action potentials

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91
Q

muscle tissue

A

skeletal (bicep), cardiac, smooth (digestive tract)

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92
Q

prokaryotes

A

cells lacking a nucleus; e.g. eubacteria and archae bacteria

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93
Q

eukaryotes

A

contain a large, membrane bounded nucleus and DNA

e.g. plants, animals, fungi, protists (algae)

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94
Q

size comparison between eukaryotic cells and prokaryotic cells

A

euk much larger than prok

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95
Q

polar amino acids

A
argenine
asparagine
glutamic acid
glutamine
histidine
lysine
serine
threonine
tyrosine
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96
Q

nonpolar amino acids

A
alanine
cycteine 
glycine
isoleucine
methionine
phenylalanine
choline
tryptophan
valine
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97
Q

what happens during sickle cell anemia

A

mutation in beta subunit and part of protein becomes hydrophobic and causes aggregation of hb molecules into a sickle shape instead of usual biconcave
glutamine (P)–> valine (NP)

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98
Q

ideal total blood cholesterol

A

200 mg/dL

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99
Q

desirable LDL levels

A

less than 130 mg/dL

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100
Q

borderline high risk of athlerosclerosis LDL levels

A

130-159 mg/dL

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101
Q

high risk of athlerosclerosis LDL levels

A

160+ mg/dL

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102
Q

what kind of ratio of HDL:LDL do you want?

A

high ratio (more HDL)

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103
Q

difference in bases between DNA and RNA

A

DNA: G-C and A-T
RNA: G-C and A-U (no T)

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104
Q

2 types of microscopy

A

light microscopy and electron microscopy

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105
Q

characteristics of light microscopy

A

glass lense, uses visible light, magnified image

resolution: 200 nm

106
Q

characteristics of electron microscopy

A

electrons magnets focus a beam of electrons on specimens, more powerful, resolution 2 nm

107
Q

types of light microscopy

A

bright field, phase contrast, stained and brightened, differential interference, fluorescence, confocal

108
Q

bright field microscopy

A

light directly passes through cells; little contrast and few details

109
Q

phase contrast microscopy

A

shows contrast by emphasizing differences in refractive index whih enhances light and dark regions and creates more contrast

110
Q

stained and brightened microscopy

A

use a stain to enhance image

111
Q

sample stains

A

eosin– binds to + structures like proteins, collagens, and muscle tissue which turns it red/pink
hematoxelyn– binds to negative structures like DNA and turns it blue/purple

112
Q

differential interference microscopy

A

2 beams of polarized light enhance contrast

113
Q

fluorescence microscopy

A

natural fluorescence; apply dye which will bind to different parts

114
Q

confocal microscopy

A

uses fluorescent materials and autofocus light to create a clearer image

115
Q

types of electron microscopy

A

transmission, scanning e-, freeze fracture

116
Q

transmission electron microscopy

A

if absorbs e- will look darker and if e- pass through, it will look lighter

117
Q

scanning e- electron microscopy

A

direct electrons to surface of sample and cause electron to be emitted where a screen catches them and produces a 3d structure

118
Q

freeze fracture electron microscopy

A

freeze cells and use a knife to crack open frozen cells and the bumps are protein aggregates

119
Q

purpose and method of cell fracturization/centrifugation

A

homogenizes cells

  1. place in tube and centrifuge
  2. particles form sediment pellet at bottom
    * heavier particles sediment at lower speeds
120
Q

centrifugation sediment times/masses

A

500 g for 10 min –> obtain nuclear fraction
10,000g for 20 min –> obtain mitochondria
100,000g for 1 hour –> get ER fraction

121
Q

what did miller and urey do?

A

conducted an experiment where they simulated the conditions of early erath

122
Q

what did miller and urey find from their experiment?

A

inorganic molecules could convert to important organic molecules and ultimately form life

123
Q

describe miller and urey’s experiement

A

heated a solution of gasses to simulate atmosphere of early earth, ran an electric current through it (like lightning), condensed it (like rain), and found amino acids, simple sugar, and other organic compounds

124
Q

what is the “RNA World” hypothesis

A

in a world before dna for protein synthesis, rna was used as a carrier of genetic information and to catalyze reactions

125
Q

theoretical process from RNA to DNA

A

start with rna (composed of ribose, bases, and phosphates) and some were replicable and eventually began to make catalytic proteins and eventually became double stranded DNA which survived because of the stability it provided for storage of genetic material
now: DNA uses RNA to make proteins

126
Q

hierarchical organization of life

A

atoms –> molecules –> organelles –> cells –> tissues –> organs –> orga systems –> organization

127
Q

5 properties of life

A
  1. cellular organization
  2. sensitivity/response to stimuli
  3. growth
  4. reproduction
  5. homeostasis
128
Q

are viruses alive?

129
Q

describe virus structure?

A

made up of a core of nucleic acids surrounded by a protein sheath (and sometimes a lipid envelope)
lack a cell membrane, nucleii, and organelles
can’t reproduce on own –> need host cell to replicate
do not carry out metabolism on their own

130
Q

what is cell theory

A

all organelles are composed of cells
cell is the basic building block of life –> all chemical reactions take place inside of cell
all cells arise through division of a pre-existing cell

131
Q

why are cells so small

A

as object increases in size, volume increases more rapidly than surface area and cells need large SA:V ration in order to efficiently transport nutrients and waste

132
Q

prokaryotes characteristics and examples

A
lack nucleus, DNA is coiled into a nucleoid
some have more than 1 nucleoid
small organism
dna is in direct contact with cytoplasm
E.g. eubacteria and archaebacteria
133
Q

eukaryotes characteristics and examples

A

contains a large, membrane bound nucleus (containing DNA)
typically separated into many membrane bound compartments (organelles)
larger organisms
e.g. all plants, animals, fungi, protists

134
Q

“special features” of prokaryotes (5)

A
  1. cell walls (bacteria may have peptidoglycan in them)
  2. outer membranes may enclose cell wall
  3. cyanobacteria can cerry out photosynthesis
  4. some may have flagella
  5. some have pili (used for mating)
135
Q

“special features” of eukaryotes (3)

A
  1. plasma membranes, cytoplasm, ribosomes
  2. internal cytoskeleton (maintains shape and moves materials around cell)
  3. plants have cell walls and large vacuoles for storage of food, water, waste, nutrients, etc
136
Q

sizes of plant cells

A

5-30 micrometers

137
Q

sizes of animal cells

A

35-80 micrometers

138
Q

sizes of prokaryotes

A

0.2-2 micrometers

139
Q

endosymbiotic theory

A

explains origin of eukaryotic cels from prokaryotic cells – states that some of the key organelles originated as a symbiotic relationship between 2 prokaryotes (one ingested other and eventually couldn’t survive without)

140
Q

what is the biggest organelle?

141
Q

what does the nucleus contain

A

most of the cells dna

142
Q

how does the nucleus faciltate replication

A

DNA combined proteins form chromatin
chromatin condenses and coils tightly to form chromosomes connected by a centromere
mitosis to form 2 daughter chromosomes

143
Q

what do chromosomes contain

A

contains one long molecule of dna - comprises many genes

144
Q

what do ribosomes do

A

synthesize proteins (all cells synthesize them on ribosomes)

145
Q

where are ribosomes located in eukaryotes (2 locations)

A

in the cytoplasm (free)

bound to the rough ER

146
Q

where do higher numbers of ribosomes go

A

energy producing organelles like the mitochondrial matrix and chloroplast stroma)

147
Q

what are ribosomes made of?

A

ribosomal RNA associated with a proton

148
Q

2 parts of the endomembrane system

A
  1. golgi apparatus

2. endoplasmic reticulum (ER)

149
Q

what is the ER

A

endoplasmic reticulum - extensive system of folded membranes

150
Q

2 parts of the ER

A

rough ER

smooth ER

151
Q

characteristics of the smooth er

A

lacks ribosomes, site for glycogen hydrolysis, synthesis of steroids

152
Q

characteristics of rough er

A

contains ribosomes, manufactures proteins for export from the cell and incorporate into membranes or to different organelles

153
Q

what does the golgi apparatus do?

A

modifies, packages, and sorts proteins

synthesizes some sugars/polysaccharides for the cell wall

154
Q

how does the golgi synthesize sugars/polysaccharides

A

vesicles from the rough er fuse with the cis region of the golgi and secretory vesicles pinch off from the trans region

155
Q

signal sequences operation

A

approximately 25AA residue long sequence at the beginning of a polypeptide chain directs the polypeptide chain to the ER and then it goes to the golgi and the secretory vesicle sends it out of the cell

156
Q

example of signal sequence

157
Q

how does insulin work

A

acts to decrease blood glucose by increasing glucose uptake in cells
the secretory vesicles are then exocytosed and stored in pancreatic beta cells until needed

158
Q

what triggers insulin release

A

an increase in blood glucose - hyperglycemia

159
Q

nickname for mitochondria

A

powerhouse of the cell

160
Q

what do mitochondria do

A

convert energy from food to ATP

161
Q

how are mitochondria sized

A

pretty small - similar in size to bacteria

162
Q

what contains mitochondria?

A

almost all living things except those living in an environment without O2

163
Q

where do most mitochindria exist

A

in metabolically active areas - heart, liver

164
Q

what are plastids present in

A

plants and some protists like algae

165
Q

what do plastids do?

A

carry out photosynthesis

166
Q

structure of plastid membrane

A

double membrane without cristae; inner membrane forms stack of thylacoids (grana)

167
Q

what is contained in thylacoid membranes

A

chlorophyll

168
Q

what is stroma

A

fluid contained within the inner membrane of chloroplasts that suspends ribosomes, dna, elara

169
Q

what are lysosomes

A

contain hydrolytic (digestive) enzymes, participate in phagocytosis

170
Q

example of a pathology of lysosomes

A

tay sachs disease

171
Q

what is tay sachs disease

A

harmful lipids known as gangliosides accumulate in dangerous quantities in the brains heme cells and the lysosomes cannot break down the compound

172
Q

what are peroxisomes (in plants and animals)

A

accumulate toxic peroxides such as H2O2

(byproduct of some biochemical reactions); and safely break it down without mixing with other parts of the cell

173
Q

glyoxysomes

A

occur in plants and are similar to perixisomes

174
Q

what are vacuoles

A

present in plant cells; store waste products and provide turgor

175
Q

what replaaces lysosomes in plants

A

vacuoles provide similar role and turgor provided keeps plant rigid

176
Q

what is the Cytoskeleton

A

maintains cell shape, facilitates cell movement

177
Q

what is the Cell wall and where is it found

A

supports the cell’s shape; present in plants, fungi and some protists (also present in bacteria)

178
Q

what is the Extracellular matrix?

A

surrounds animal cells, and is composed of proteins eg. collagen,
glycoproteins, and proteoglycan

179
Q

3 Components of the cytoskeleton

A

microfilaments, intermediate filaments, and microtubules

180
Q

what are microfilaments?

A

strands of actin, involved in movement during animal cell division, and muscle contraction

181
Q

3 uses for microfilaments

A

a. muscle contraction (myosin and actin interactions)
b. cytokinesis (division of cytoplasm)
c. microvilli (epithelial lining of small intestine); increase surface area for absorption
of nutrients across lumen across to the blood

182
Q

what are intermediate filaments and an examples

A

tough, fibrous protein molecules twisted into rope-like structures which stabilize cell structure e.g. keratin in hair/nails

183
Q

what are microtubules

A

involved in structure and function of cilia and flagella, centrioles, and movement of cellular organelles; important for the mitotic spindle;

184
Q

microtubule uses

A

scaffolding

185
Q

what is the sturcture of microtubules

A

hollow cylinders made of tubulin; made up of tubulin alpha and beta subunits- 13 subunits arranged in circle

186
Q

what happens during depolymerization of microtubules

A

pull sister chromatids to opposite poles of cell

187
Q

what are cilia

A

9 sets of microtubules arranged in spoke like pattern (9+2 pattern)

188
Q

what are CENTRIOLES

A

microtubule organizing structure

189
Q

what are Motor proteins and examples

A

use energy from ATP to use microtubules and facilitate movement of cell e.g. dynein and kinesin

190
Q

how do flagella move?

A

Complex protein ring structures anchored in the plasma membrane form a motor unit that rotates the flagellum and propels the cell

191
Q

how do Sister chromatids separate to form chromososmes

A

Mitotic spindle microtubules from opposite poles attach to each sister chromatid at the kinetochore in prometaphase. In anaphase, the connection between the sister chromatids breaks down and the microtubules pull the chromosomes toward opposite poles.

192
Q

golgi apparatus cis region

A

lies closest to nucleus

193
Q

where is the golgi apparatus trans region?

A

closer to cell surface

194
Q

what act as the target for the signal sequences to latch onto

195
Q

pH inside a lysosome

A

acidic - 5.5

196
Q

what is autophagy

A

breaking down worn out cell organelles

e.g. worn out mitochondria could fuse with a lysosome and be broken down

197
Q

what are glyoxysomes

A

in plants, specialized form of peroxisomes; break down stored lipids
no lysosomes in plants

198
Q

how do microfilaments participate in cytokinesis (division of cytoplasm)

A

occurs by loops of actin (microfilaments, which can lengthen or shorten by adding or subtracting individual actins) forming around the middle

199
Q

why are microtubules important to the mitotic spindle

A

attach to sister chromatids during cell division; pull them apart and reform the nucleus

200
Q

size progression of cytoskeleton components

A

(smallest) microfilaments –> intermediate filaments –> microtubules (largest)

201
Q

what type of cell lines the small intestine

A

endothelial cells

202
Q

what are microvillus

A

projections used to absorb nutrients, increases surface area for absorption from lumen of gut

203
Q

what are cilia made of and why are they important

A

9 microtubules; important in airway which prevent particles from getting into lungs

204
Q

what causes fluidity of lipid bilayer

A

movement of individual phospholipids

205
Q

what are membrane proteins

A

Carry out most of specific functions

Amount and types of proteins in a membrane are variable

206
Q

3 classes of membrane proteins

A

integral, peripheral, and lipid-anchored proteins

207
Q

integral proteins

A

(penetrate into the lipid bilayer) - most are transmembrane proteins (contain an alpha-helix of nonpolar amino acids extending across the hydrophobic interior of the membrane)

208
Q

peripheral proteins

A

located outside of the lipid bilayer on the cytoplasmic surface attached by noncovalent bonds to the polar head groups of the lipid bilayer, or to integral membrane proteins

209
Q

lipid-anchored proteins

A

covalently attached to a phospholipid or fatty acid embedded in the bilayer

210
Q

Role of membrane proteins (3)

A

transport proteins
receptors for molecular messengers from other cells
form junctions between cells

211
Q

what are MEMBRANE CARBOHYDRATES

A

Project from the exterior surface of the plasma membrane when attached to proteins or phospholipids within the membrane
Serve as recognition sites on the cell surface

212
Q

what are glycoproteins

A

carbohydrates (oligosaccharides) in membranes bound to proteins that enable cells to recognize foreign substances

213
Q

what are glycolipids

A

form cell identity markers eg. A,B, O blood group markers

214
Q

types of cell junctions

A

tight junctions
desmosomes
gap junctions

215
Q

why are gap junctions important in the heart

A

allow small molecules (e.g. iron) to move from cell to cell

facilitates spread of action potentials (what tells the heart to beat)

216
Q

what are plasmodesmata

A

aqueous pore in plant cells - analogous to gap junctions

217
Q

what anchors extracellular matrix to exterior cytoskeleton and what is it attached to

A

integrin and attached noncovalently to fibronectin

218
Q

what type of mechanism is an ion channel and how does it work

A

passive and nonmediated - creates an aqueos pore in the membrane

219
Q

what type of mechanism is a carrier (transporter) and how does it work

A

passive and carrier mediated; carrier protein allows polar molecule to shuttle through
no aqueous pore is created
moves from high to low - facilitated by mechanism, but still passive because does not require to move against concentration gradient

220
Q

what is diffusion

A

random molecular motion from areas of high concentration to lower concentration

221
Q

what type of mechanism would move molecules against the concentration gradient

A

active, mediated transport involving a membrane protein carrier and requiring energy

222
Q

what can diffuse across the lipid bilayer

A

Small nonpolar molecules, e.g. O2 and CO2

223
Q

what is osmosis

A

Diffusion of water molecules across a selectively permeable membrane

224
Q

why can’t plant cells burst like animal cells can

A

stability from the cell wall

225
Q

what is osmolarity

A

sum of ions in solution

226
Q

benchmark osmolarity of blood plasma and hyposmotic and hyperosmotic

A

~300 mosmol/L

300

227
Q

what regulates channel proteins

A
  1. binding of some specific molecule (ligand gated)

2. change in voltage (voltage gated)

228
Q

graphs of diffusion to see if it experiences saturation kinetics

A
  1. linear would indicate it’s not carrier mediated and is 2. simple diffusion (does not experience saturation kinetics)
    curved and eventually flattening out means it can saturate andyou will reach max rate of transport
229
Q

uniport

A

molecule moves one direction

230
Q

symport

A

molecules move same direction

231
Q

antiport

A

molecules moving in opposite directions

232
Q

what does Endocytosis do

A

transports macromolecules, large particles and small cells into eukaryotic cells

233
Q

3 types of endocytosis

A

Phagocytosis, Pinocytosis, and Receptor-mediated endocytosis

234
Q

what is phagocytosis

A

large particles or cells are engulfed

235
Q

what is pinocytosis

A

small dissolved solutes or fluids enter

236
Q

what is Receptor-mediated endocytosis

A

a specific membrane receptor binds to a particular macromolecule at sites called coated pits

237
Q

what is endocytosis

A

taking molecules into cells

238
Q

what is exocytosis

A

vesicle fusing and dumping outside

239
Q

what is an exergonic reaction

A

A reaction whose products contain less free energy than the reactants (delta g is negative); tend to occur spontaneously and release heat; catabolism – cell respiration

240
Q

what is an an endergonic reaction

A

products of the reaction contain more energy than the reactants and the extra energy must be supplied for the reaction to occur; anabolism – active transport and cell movements

241
Q

what is the main carbohydrate store in humans

242
Q

what is the main lipid store in humans

A

triglycerides

243
Q

what does metabolism do to energy stores

A

breaks it down into ATP

244
Q

2 ways cells make atp

A

substrate-level phosphorylation

chemiosmosis (most do this way)

245
Q

how does substrate-level phophorylation work?

A

direct transfer of phosphate group to ADP from another molecule

246
Q

why does breaking atp bonds release so much energy

A

it has negatively charged phosphates which are close to each other which takes a lot of energy, so breaking those binds releases lots of energy

247
Q

is atp actually a nucleotide?

248
Q

how do autotrophs synthezise food molecules

A

using light energy

249
Q

do heterotrophs or autotrophs extract energy from food?

A

trick! both do

250
Q

stages of extracting energy from food

A
  1. digestion - enzymes break large moleucles into smaller molecules
  2. catabolism - other enzymes dismantle fragments extracting energy at each stage
251
Q

what is harvested to generate ATP

A

Glucose (C6H12O6); C-H bonds; uses the energy from the electrons making up the bonds

252
Q

what is glycolysis

A

conversion of glucose to pyruvate

253
Q

what is cellular respiration

A

conversion of pyruvate to CO2 and water in the presence of O2 which releases large amounts of energy

254
Q

where does chemiosmosis occur

A

mitochondria

255
Q

where did the term oxydative phosphorylation come from?

A

experiment where mitochondria were put in a test tube with ADP and phosphate and oxygen and it makes ATP

256
Q

what is the more current/accurate way to describe making ATP

A

chemiosmosis (in mitochondria)

257
Q

which organelle can you use the terms chemiosmosis and substrate level phosphorylation intrchangeable and which ones can you not

A

mitochondria can use both, but chloroplasts cannot

258
Q

how is atp generated by substrate-level phosphorylation

A

Involves direct transfer of phosphate group to ADP from another molecule

259
Q

how is atp generated by chemiosmosis

A

glucose enters cells, converted to pyruvate, converted to CO2

260
Q

what is NAD+

A

an electron shuttle; AN ELECTRON CARRIER IN MANY REDOX REACTIONS; Nicotinamide adenine dinucleotide