Unit 2 Flashcards

1
Q

do signal sequence, RNA-protein particle, preceptor, and channel work for any protein?

A

yes they are all generic

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2
Q

where are proteins sent once they are processed inside ER

A

golgi

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3
Q

how do finished proteins from ER travel to golgi

A

through tubes that extend from ER and grow along microtubules

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4
Q

what 2 things happen once proteins and lipids are inside golgi

A
  1. undergo final modifications
  2. sorted into compartments that correspond to certain destinations in cell
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5
Q

how do vesicles get to their destination

A

exterior of each vesicle membrane has proteins that act like zip codes
motor proteins like kinesin walk along microtubule

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6
Q

what does the endomembrane system consist of

A

ER, golgi, secretory vesicle, endosome, lysosome

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7
Q

function of ER

A

protein folding and modifications

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8
Q

function of golgi

A

further modifications and sorted into compartments

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9
Q

function of secretory vesicle

A

motor proteins direct vesicle to destination, soluble proteins released

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10
Q

function of endosome

A

destination, materials brought in by endocytosis and released by exocytosis

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11
Q

function of lysosome

A

path of newly synthesized digestive enzymes, site of degradation

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12
Q

how do proteins get to their correct cellular location

A

3 mechs:
1. transport through nuclear pores
2. transport across membranes
3. transport by vesicles

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13
Q

what are signal sequences

A

short sequences of amino acids that direct proteins to locations

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14
Q

each location is targeted with a ____ signal sequence

A

specific

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15
Q

does constitutive secretion occur continuously

A

yes

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16
Q

how are integral membranes inserted into ER membrane

A

co-translational translocation

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17
Q

describe the process for co-translational translocation

A

SRP pauses translation, SRP binds to receptor and translation resumes, ribosome binds to translocator, plug moves, signal sequence binds to translocator, translocation continues and protein is translocated into lumen of ER where signal sequence is cleaved, signal sequence degrades and plug closes translocator

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18
Q

hydropathy

A

amount of free energy required to move sequence of amino acids from nonpolar solvent to water

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19
Q

ATP has extremely ___ potential energy

A

high

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20
Q

endergonic rxn is ___

A

nonspontaneous, increase in free energy

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21
Q

exergonic is ____

A

decrease in free energy, spontaneous

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22
Q

what affect does spatial orientation have on enzymes

A

makes it unlikely for reactants to bump into each other at random

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23
Q

where do reactants move around

A

cytosol or interior of organelle

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24
Q

what is activation energy

A

as old bonds break and before new bonds form, there is transition state where reacting substances are much less stable than before rxn started

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25
Q

if the reaction is less stable, what happens to free energy

A

it spikes

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26
Q

do enzymes change free energy of reactants or products

A

no

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27
Q

what is unique about enzymes

A

each enzyme catalyzes one particular rxn bc size, shape, and chem composition of active site is so that reactants fit into space and bind to R-groups

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28
Q

what is the most accurate velocity when looking at rate of rxn

A

initial velocity of enzyme-substrate rxn bc rxn rate will decrease as substrate is made into product

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29
Q

why does plateau occur

A

bc enzyme is saturated so all available enzyme molecules are processing substrates

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30
Q

what is the rate of rxn limited by

A

concentration of enzyme

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31
Q

what is Vmax

A

max rate of rxn of particular enzyme at particular concentration, occurs when enzyme is saturated

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32
Q

what does it mean when an enzyme is saturated

A

all active sites are occupied by substrates

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33
Q

what is Km

A

substrate concentration that gives a rate that is halfway to Vmax, helps measure how quickly rxn rate increases with substrate concentration, measures enzyme affinity for binding to its substrate

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34
Q

lower Km = ____ affinity

A

higher

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35
Q

what is Kcat

A

turnover number, (Vmax)/[enzyme]

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36
Q

an enzyme that has a high efficiency would have what kind of values for Km and Kcat

A

low Km and high Kcat

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37
Q

Michaelis-Menten kinetics equation

A

E + S –> [ES] –> E + P
V = (Vmax x [S])/(Km + [S])

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38
Q

what is steady-state assumption

A

concentration of enzyme-substrate complex is constant over time
[ES] = constant

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39
Q

what is initial-velocity assumption

A

initial rate of rxn is measured so concentration of substrate is much higher than concentration of product

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40
Q

what is single-substrate assumption

A

assumes that enzyme-catalyzed rxn involves single substrate interacting w enzyme to form ES complex

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41
Q

what is reversibility assumption

A

reverse rxn of substrate dissociating from ES complex to form enzyme and substrate again is negligible under typical conditions

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42
Q

what is substrate concentration

A

[S]»[E] so that [S] is constant when measuring instantaneous velocity

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43
Q

what is an activator

A

molecules that increase activity of enzyme

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44
Q

what is an inhibitor

A

molecules that decrease activity of enzyme

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45
Q

what is noncompetitive inhibition

A

inhibitor and substrate can both be bound at same time

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46
Q

what happens to Vmax and Km in presence of competitive inhibitor

A

Vmax is unchanged, Km is higher

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47
Q

what happens to Vmax and Km in presence of noncompetitive inhibitor

A

Vmax is decreased, Km is unchanged

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48
Q

what type of rxn drives ATP production

49
Q

what is electrical energy

A

flow of currents/flow of charge, used to drive molecular motors that use mech energy to product ATP

50
Q

list the major steps in cellular respiration

A

glycolysis, pyruvate processing, citric acid cycle, e- transport chain, ATP synthase

51
Q

how many ATP does glycolysis produce

52
Q

what reactant does glycolysis begin with

53
Q

what does glycolysis end with

A

2 pyruvate

54
Q

where does pyruvate processing happen

A

single multi-unit enzyme complex

55
Q

what does pyruvate start with as a reactant

56
Q

what does pyruvate processing produce

A

acetyl coenzyme A, oxidized 2 of carbons in glucose to CO2

57
Q

what does citric acid cycle begin with

A

acetyl-CoA

58
Q

how much ATP does citric acid cycle produce

59
Q

ETC uses ___ and yields ___ as product

A

oxygen; water

60
Q

what does ATP synthase convert ADP and inorganic phosphate into

61
Q

what is oxidative phosphorylation

A

ATP production at end of cellular respiration

62
Q

what are the 2 e- carriers

A

NADH and FADH2

63
Q

what organelle does cellular respiration involve

A

mitochondrion

64
Q

ETC is collection of multiple proteins embedded in ___ mitochondrial membrane

65
Q

in complex I, what happens to NADH

A

it becomes NAD+

66
Q

in complex II, what happens to FADH2

A

it becomes FAD

67
Q

what is the final e- acceptor in ETC

68
Q

if one part of the assembly line stops, what happens to ETC

A

e- can’t move to next position, energy stops getting released, no more proton pumping can happen

69
Q

ATP synthase is complex V and the flow of current is carried by protons to a ___ that spins turbine that produces ATP

70
Q

where do protons enter complex V

A

F0 subunit, making ATP synthase spin

71
Q

what does the twisting force in ATP synthase do

A

causes F1 subunit to change shape to catalyze addition of phosphate group to ADP, forming ATP

72
Q

which is more efficient: fermentation or cellular respiration

A

cellular respiration

73
Q

how does fermentation work

A

pathway that transfers e- from NADH to carbon-based molecule to regenerate NAD+ and keep glycolysis running to produce small amounts of ATP

74
Q

diff between anaerobic and aerobic respiration

A

anaerobic: e- reduce substances other than oygen (SO42-, CO2, NO3-, NO2-)
aerobic: oxygen acts as final e- acceptor in ETC

75
Q

catabolic pathways ___ molecules

A

break down

76
Q

anabolic pathways ____ molecules

A

build and create

77
Q

allosteric regulation

A

regulatory molecule (activator or inhibitor) binds to enzyme someplace other than active site

78
Q

what is the site called when regulatory molecule binds to enzyme someplace other than active site

A

allosteric site

79
Q

almost all cases of noncompetitive inhibition are forms of _____ regulation

A

allosteric

80
Q

allosteric activation

A

activation of enzyme’s activity by molecule binding to allosteric site

81
Q

allosteric enzymes

A

have multiple active sites located on diff protein subunits

82
Q

cooperativity

A

substrate itself can serve as allosteric activator, when it binds to one active site the activity of other active sites increase

83
Q

cofactors

A

non-protein helper molecules that can attach temporarily to enzymes through ionic or hydrogen bonds or permanently through stronger covalent bonds

84
Q

many enzymes don’t work optimally or at all unless bound to ___

A

cofactor (ex. Fe2+, Mg2+)

85
Q

coenzymes

A

subset of cofactors that are organic molecules (Vitamin C)

86
Q

what does compartmentalization enable

A

segregation of enzymes involved in diff metabolic pathways, regulating cellular processes

87
Q

feedback inhibition

A

end product of metabolic pathway acts on key enzyme regulating entry to that pathway so that it keeps more of end product from being produced

88
Q

can the cell turn off its own pathway to ensure it makes the right amount of product

89
Q

what happens if there’s little product

A

enzyme won’t be inhibited and pathway will continue to replenish

90
Q

what happens if there’s lots of product

A

cell will block enzyme and prevent production of new product until existing supply is used up

91
Q

what catalyzes pathway steps regulated by feedback inhibition

A

allosteric enzymes

92
Q

what happens to cellular respiration when oxygen is depleted

A

O2 cannot accept e- at end of ETC, e- build up in ETC and e- can’t enter, NADH and FADH2 build up so NAD+ isn’t available for glycolysis

93
Q

fermentation allows cells to regenerate ___

94
Q

what is reduced and oxidized in fermentation

A

pyruvate is reduced, NADH is oxidized

95
Q

what is produced for 1 glucose molecule

A

2 ATP, 2 lactate, 2 NAD+ generated

96
Q

what is metabolic flux

A

movement of metabolite through pathway over time

97
Q

reversible rxns have change in free energy close to ___

98
Q

irreversible rxns have change in free energy ___ zero

99
Q

true or false: metabolic pathways never come to equilibrium bc free energy is required to do work

100
Q

what is the equation for photosynthesis

A

CO2 + H2O + light energy –> carbohydrate + O2

101
Q

what is oxidized in photosynthesis

102
Q

what is reduced during photosynthesis

A

carbon atom

103
Q

what is first stage in photosynthesis

A

energy in specific wavelengths of light is absorbed by pigments which causes e- to be excited in high-energy state

104
Q

what happens in PSII

A

excited e- are passed to molecule called PQ (reducing it), transforms light energy to chem energy

105
Q

what does PQ do once excited e- are passed to it

A

carries e- out of PSII and passes it to ETC to pump protons across membrane

106
Q

describe stage 2 of photosynthesis

A

pigment molecules in PSI, excited e- passed through series of carriers until they reach enzyme that uses energy to catalyze reduction of NADP+, completes transformation of light energy captured in PSI to chem energy
NADPH is e- carrier and reduced form of NADP+

107
Q

what happens in stage 3 of photosynthesis

A

ATP and NADPH produced from energy kept in PSII and PSI are used in Calvin cycle that results in reduction of CO2 to produce sugars

108
Q

where are PSII, ATP synthase, PSI found

A

chloroplasts, membranes of flattened sacs so there is high proton concentration

109
Q

what does the Calvin cycle begin with

A

CO2 added to 5-carbon sugar

110
Q

what does Calvin cycle produce

111
Q

what is rubisco

A

enzyme that catalyzes first step in calvin cycle

112
Q

how does rubisco work

A

attaches to CO2 molecule to 5-carbon sugar that is regenerated at end of each turn in cycle

113
Q

what does rubisco produce

A

2 identical molecules of 3-carbon sugar

114
Q

what does rubisco catalyze the reduction of

115
Q

true or false: rubisco is most abundant enzyme on earth

116
Q

what happens when CO2 levels in chloroplast are low

A

O2 can bind to active sites and be added to 5-carbon sugar that acts as substrate

117
Q

how does CO2 get to chloroplasts

A

plant stems covered with wax blocks movement of water away from plant and keeps stems and leaves from drying out; stems and leaves have openings called stomata in epidermis that aren’t covered in wax where CO2 can diffuse in and O2 diffuse out

118
Q

what regulates size of stomata

A

specialized guard cells

119
Q

where does plant mass come from

A

CO2 in air