Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochem > Exam 1: M1&2 > Flashcards

Exam 1: M1&2 Flashcards

1
Q

T/F: cells are densely packed w macromolecules

A

T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Do bacteria have nucleosomes

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what are the 4 classes of biological polymers

A

Proteins
polysaccharides/carbohydrates
lipids
nucleic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is the largest/most diverse biological polymer class

A

proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

are lipids true biological polymers

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

polysaccharides can be ___ or ____

A

linear, branched

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

nucleic acids consist of ___ and ___

A

DNA, RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what are the characteristics of CHNOPS

A

small, stable, 4 val e-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

3 main molecular forces in macromolecules

A

covalent, noncovalent, hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Noncovalent bonds in order of inc strength

A

van der waals, H bonds, ionic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

strongest molecular force

A

covalent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

ion pairs are highly susceptible to …

A

pH bc pH affects charge state

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

dipole-dipole interactions are between ___ molecules

A

neutral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what causes a dipole-dipole interaction

A

e- cloud not very distributed, dependent of separation of charges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what do H bonding need

A

electron acceptor and donor; direction is important

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

distance for ion pair bonding

A

3-10 angstrom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

dipole-dipole distance

A

3-10 angstrom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

H bonding distance

A

1.5-2 angstrom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

T/F: Van der waals is in all macromolecules/atoms

A

T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

distance of van der waals

A

3-5 angstrom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

T/F: van der waals can be strong collectively

A

T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what drives hydrophobic interactions

A

entropy of water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

entropically, more organized arrangement of water molecules around surface of hydrophobic molecules is ____

A

unfavorable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

more organized water around surface of hydrophobic molecules is unfavorable so…

A

hphobic molecules come together and reduce overall surface area of hydrophobic molecules which lets water molecules be more random in soln

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

hphobic interactions are an ____ effect

A

exclusion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how is entropy a driving factor of hphobic interactions

A

entropic cost of arrangement of water molecules; they have to be very ordered on hphobic molecules surface. interactions will give less surface area

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

examples of how hphobic interactions are important

A

membranes and amphipathic molecules, diff macromolecules interacting for protein folding and formation of diff types of membranes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Features of biological polymers

A

directional, informational, structured in 3D

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

how do we build biopolymers

A

condensation reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

T/F: not all chemical reactions happen in equil

A

F

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

properties of water

A

polar, non-linear, bent, H bond donor and acceptor, can form 4 H bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

what makes water a good solvent

A

irregular network of H bonded molecules, soluble for ionic and other polar molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

T/F: strength of an acid is specificed by its dissociation constant

A

T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

pK is the -log of the ___?

A

dissociation constant

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

when pH<pka…

A

protonated form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

when pH>pKA…

A

deprotonated form

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

pH=pK when

A

half the molecules are protonated and other half is deprotonated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

pK depends on ___?

A

molecular structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

acid next to a positive charge will inc or dec pk?

A

dec

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

base close to hydrophobic pathc will inc or dec pk?

A

inc

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

acid close to hydrophobic patch will inc or dec pk?

A

dec

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

blood ph

A

7.35-7.45

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

how to pick a buffer for a rxn if we want to mimic the cellular env?

A

pk of buffer must be close to pH rxn occuring in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

first law of thermodynamics

A

energy is conserved and is primarily concerned w enthalpy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

second law of thermodynamics

A

entropy inc toward a state of disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

T/F: rxns don’t have to be spontaneous to occur

A

F

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

gibbs free energy is a measure of…

A

spontaneity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

spontaneity doesn’t predict anything about

A

kinetics/rate/speed of rxn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

At equil, delta G =

A

0

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

delta G is independent of

A

rxn mechanism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

delta G is influenced by ?

A

changes in free energy of products and reactants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

endergonic

A

nonspont.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

exergonic

A

spont.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

+deltaH, +deltaS

A

spont when T> deltaH/deltaS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

+deltaH, -deltaS

A

nonspont at all temps

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

-deltaH, -deltaS

A

spont when T < deltaH/deltaS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

-deltaH, +deltaS

A

spont at all temps

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

delta g is ___ ____?

A

rxn specific

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

delta g depends on…

A

conc of reactants of products

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

free energy changes depends on ___ and on ___ of reactants and products

A

rxn taking place; concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

free energy is a function of change in ___?

A

entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

proteins are polymers of ?

A

aa

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

4 key components of aa

A

alpha carbon, amine group. carboxyl group, R group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

pk of amino group of aa

A

9.4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

pk of carboxylic acid of aa

A

2.2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

all aa in proteins are in ____

A

L

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

at physiological pH, aa are ___

A

charged

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

peptide bonds are ___ and ___ than typical C-C bonds

A

shorter; stronger

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

backbone is ___, _____, and _____

A

hydrophilic; soluble; polar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

what determines folding and chemical properties?

A

side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

acidic aa

A

aspartic acid, glutamic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

basic aa

A

histidine, arginine, lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

nonpolar/hydrophobic aa

A

phenylalanine, alanine, leucine, methionine, isoleucine, tryptophan, proline, valine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

polar/uncharged aa

A

cysteine, glycine, glutamine, asparagine, serine, tyrosine, threonine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

structurally important aa

A

proline (5 mem ring)
glycine (no R group)

both have small R groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

sulfur-containing aa

A

methionine and cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

which sulfur containing aa can’t form disulfide bridge

A

methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

which sulfur-containing aa can form disulfide bridge

A

can form disulfides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

which bonding interactions do disulfide bridges have

A

covalent linkages betwn 2 sulfhydryl groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

disulfide bridge is the ___ form of sulfhydryl

A

reduced

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

why can’t methionine form disulfide bridges

A

it doesn’t have sulfhydryl group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

alcoholic aa

A

serine, threonine, tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

which aa are targets of phosphorylation

A

alcohols

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

aromatic aa

A

phenylalanine, tyrosine, tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

where are aromatic aa usually found

A

protein interior bc they are hydrophobic from bulky sidechains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

pk of aspartic acid

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

pk of glutamic acid

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

pk of lysine

A

10.5

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

pk of arginine

A

12.5

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

pk of histidine

A

6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

what can acidic and basic aa do

A

can grab or donate a proton or make salt bridges and ion pairs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

ion pairs are common btwn ___ and ____

A

acids; bases

83
Q

at cellular pH, which side chains are + charged?

A

?

84
Q

at cellular pH, which side chains are - charged

A

?

85
Q

histidine pk

A

6.04

86
Q

at physiological pH, histidine can be ___ or ___

A

protonated; deprotonated

87
Q

pK values depend on ____ ______

A

chemical surroundings

88
Q

why is histidine special

A

pk is close to physiological ph

89
Q

N terminus pK

A

9-10

90
Q

C terminus pk

A

2-3

91
Q

what is the pI

A

pH nat which a molecule carries no net electric charge

92
Q

how to calculate pI

A

(pki + pkj) / 2

93
Q

Pi of polypeptide must be determined experimentally bc ______ dictates what the pk is

A

env of every side chain

94
Q

protein w low PI is ___

A

acidic

95
Q

protein w high pI is ____

A

basic

96
Q

which aa is neither hydrophobic or hydrophilic

A

glycine

97
Q

which aa undergo phosphorylation

A

serine, threonine, tyrosine

98
Q

which group gets replaced by what other group during phosphorylation

A

phosphate group replaces hydroxyl

99
Q

what does phosphorylation do to the side chains

A

changes charge from neutral to -2

100
Q

which aa gets hydroxylated

A

lysine and proline

101
Q

what group replaces what group during hydroxlation

A

OH replaces H

102
Q

what does hydroxylating a side chain do

A

controls activity of proteins and stabilizes certain structures

103
Q

which aa gets methylated

A

lysine, arginine, histidine

104
Q

what does methylating a side chain do

A

cell “markers”
ex. histones in chromatin controls epigenetics

105
Q

which aa gets ubiquinated

A

lysine

106
Q

how is ubiquitin linked to lysine

A

covalent bond

107
Q

how does the sanger sequencing work

A

1) start w protein purified in soln (can be one or multiple polypeptide chains linked)
2)a reducing agent is used to reduce the disulfide bonds and separate the chains
3)use proteases to get smaller pieces by fragmenting chains (use 2 diff proteases to get 2 diff sets of fragments we can overlap later)
4) sequence 1 aa at a time from N terminus of each fragment and end up w series of smaller peprides we nkow the sequence of
5) use computers to overlap diff fragments to read out overall seq

108
Q

why is protein sequencing important

A

can figure out where specific modifications are in a given chain

109
Q

define primary strucutre

A

linear sequence of aa

110
Q

define secondary structure

A

regularly repeating folding patterns (alpha helices or beta sheets)

111
Q

in secondary structure, what do patterns depend on

A

position of atoms in peptide bond

112
Q

define tertiary structure

A

overall 3D fold of a given protein, includes both atoms in backbone and R groups

113
Q

define quarternary structure

A

assembly of units

114
Q

what are restrictions to peptide bonds

A

rigid and planar bc of db character from resonance

115
Q

all a but proline are in the ____ conformation

A

trans

116
Q

which atoms is the psi angle between

A

alpha carbon to next carbon

117
Q

which atoms is the theta angle between

A

alpha carbon to N

118
Q

what determines/defines secondary structures

A

dihedral angles

119
Q

how do we know what psi and theta angles are allowable for given aa sequences

A

ramachandran plots

120
Q
A
121
Q

allowable theta angles

A

-60 to -150

122
Q

___ is the most flexible/least sterically hindered aa bc it lacks typical R group

A

glycine

123
Q

___ is the most restricted/most sterically hindered aa bc it has a cyclical ring

A

proline

124
Q

extensive ___ bonding along peptide backbone

A

H

125
Q

n and n+? residue pattern for alpha helix

A

4

126
Q

distance btwn residues (up and down) for helix

A

1.5A

127
Q

which atoms in the aa are h bonded

A

H on amide N to O from carbonyl

128
Q

how many resides per turn

A

3.6

129
Q

distance for one full turn of helix (pitch)

A

5.4A

130
Q

sidechains project out and ___

A

down

131
Q

what interactions stable core of helix

A

van der waals

132
Q

how do r groups give rise to structure

A

r groups not physcially interacting through H bonding or any other force w the atoms in the backbone so not contributing the helix physically but do dictate allowable theta and psi angles which determine if a given pepride can fold into helix or sheet

133
Q

distance btwn residues for sheets

A

3.5A

133
Q

beta sheets have theta and psi angles much cloesr to ___

A

180 degrees bc more extended structure

133
Q

In sheets, H bonding occurs between

A

neighboring chains

134
Q

in beta sheets, every successive aa faces ___ _____

A

in opposite directions

135
Q

every ___ aa forms same face of beta sheet

A

other

136
Q

in antiparallel beta sheet, H bonding occurs btwn

A

H of amide and O of carbonyl

137
Q

parallel beta sheets aren’t as stable bc

A

H bonding isn’t in perfect register like they are in antiparallel sheets

138
Q

secondary structure is stabilized primarily by ___

A

H bonding

139
Q

secondary structure doesn’t usually involve

A

side chains

140
Q

alpha helices and beta sheets are connected to each other by tight ___ or flexible ___

A

turns;loops

141
Q

other secondary structures include

A

reverse turns (not a true secondary structure) and polyproline helix (true secondary structure)

142
Q

reverse turns are often found on

A

protein surface

143
Q

what defines reverse turns

A

n and n+3

144
Q

T/F: alpha helices are tighter than reverse turns

A

F

145
Q

reverse turns usually have ___ at residue 2 in type 1

A

proline

146
Q

reverse turns usually have ___ at residue 2 in type 2

A

glycine (to avoid steric clash)

147
Q

polyproline helix has ____ H bonding

A

unusual

148
Q

what is polyproline helix found in

A

collagen

149
Q

what is the aa composition of a polyproline helix

A

33% glycine, 15-30% proline, and Hyp

150
Q

what define a polyproline helix

A

repeating sequences of gly-Pro-Hyp

151
Q

what interactions are involved w polyproline helices

A

van der waals, H bonding

152
Q

what is Hyp

A

modified version of proline

153
Q

the enzyme necessary to modify prline to make Hyp requires __?

A

vitamin c

154
Q

T/F: polyproline helices are v diff than alpha helices

A

T

155
Q

each indiv polyproline helix is

A

left handed

156
Q

collagen triple helix is

A

right handed

157
Q

1 polyproline helix

A

left handed
3 residues per turn
van der waals stabilized
proline prevetns formation of alpha helix

158
Q

collagen

A

3 polyproline helices
right handed
H bonding btwn H of amide group of glycine to carbon of carbonly of proline

159
Q

what dictates secondary structure

A

protein sequence

160
Q

acidic residues are what color

A

red

161
Q

basic residues are what color

A

blue

162
Q

hydrophobic/ nonpolar is what color

A

white

163
Q

a very basic patch will be (?) charged and will want to bind to (?)

A

(+); (-)

164
Q

define tertiary structure

A

overall 3D shape of protein and fold

165
Q

what determines tertiary structure

A

linear sequence of aa

166
Q

T/F: hard to predict overall 3D shape of protein based on primary aa sequence

A

T

167
Q

3 classifications of proteins

A
  1. globular
  2. fibrous
  3. membrane
168
Q

characteristics of globular proteins

A

soluble, compact
ex: myoglobin, hemoglobin

169
Q

for globular proteins, where are hydrophobic residues

A

protein interior

170
Q

for globular proteins, where are hydrophilic residues

A

protein surface

171
Q

characteristics of fibrous proteins

A

regular repeating elements
makes elongated structures

172
Q

fibrous proteins form…

A

protective connective structures like keratin or collagen

173
Q

membrane proteins are very

A

hydrophobic

174
Q

for membrane proteins, hydrophobic residues are on

A

surface

175
Q

for membrane proteins, hydrophilic residues are on

A

protein interior

176
Q

tertiary structures (globular) stabilize by

A

hydrophobic effect

177
Q

densely packed core of globular protein is stabilized by

A

van der waals

178
Q

the 7 supersecondary structures

A
  1. BaB
  2. B hairpin
  3. aa motif (coiled coil, helix bundles)
  4. greek key motif
  5. helix loop helix
  6. helix turn helix
  7. zinc finger domain
179
Q

BaB supersecondary structure

A

parallel B sheets that are connected by alpha helix;
important in Rosmann fold

180
Q

B hairpin supersecondary structure

A

antiparallel B sheets connected by tight turns; beta barrels

181
Q

aa motif supersecondary structure

A

2 alpha helices tilted but connected by loop or turn

182
Q

Greek key motif supersecondary structure

A

mutliple antiparallel beta sheets aligned w one another; ex beta cliftolin

183
Q

helix loop helix

A

one helix connected to another by a loop;
can be oriented diff;
interact w IMF

184
Q

helix turn helix

A

one helix connected to another by a reverse turn

185
Q

loops vs. turns

A

loops are longer and more flexible (10-20aa) turns are tight and not flexible (3-4 aa)

186
Q

zing finger domain

A

25-60 aa arranged around 1 or 2 zinc ions; Zn tetrahedrally coordinated to 4 aa side chains;
involved w genome editing

187
Q

define a domain

A

w/in a polypeptide chain, indiv folded units structurally independent

188
Q

T/F: each domain has discrete functions

A

T

189
Q

many proteins have multiple folded domains connected by flexible ____

A

linkers

190
Q

domains vs subunits

A

w/in one subunit can have multiple domains; 1 polypeptide chain = subunit which can have multiple domains

191
Q

define quaternary structure

A

arrangement of indiv subunits wrt one another

192
Q

T/F: diff subunits are often covalently linked together

A

mostly F; use noncovalent forces (hphobic, salt bridges, VDW, H bonding) but sometimes covalently linked via disulfide bonds

193
Q

T/F: proteins are in equilibrium w folded and unfolded state

A

T

194
Q

T/F: equilibrium favors unfolded state

A

F

195
Q

which side chains are most mobile

A

lysine, arginine

196
Q

intrinsically disordered proteins are rich in ___

A

polar/charged aa–> glutamine, serine, glutamate, llysine, glycine, alanine

197
Q

proteins are sensitive to:

A

heat, pH, detergetns, chaotropic agetns, reducing agetns

198
Q

what are the chaotropic agents

A

urea, guanodidium

199
Q

reducing agents break apart

A

disulfide bonds

200
Q

a protein is only ____ KJ/mol more stable in folded state relative to unfolded state

A

40

201
Q

a. single H bond is __ KJ/mol

A

20

202
Q

small free energy difference allows proteins to be ___

A

dynamic

203
Q

protein folding is a ____ process

A

reversible

204
Q

what did Anfinfsen’s experiment show with RNaseA

A

all the info you need to fold a protein is encoded in primary sequence

205
Q

describe the RNase A experimental steps

A

add urea and mercaptoethanol to denature protein and break disulfide bonds

dialyze away urea + mercaptoethanol which renatures the re-forms the disulfide bonds in presence of O2

206
Q

what drives proteins folding

A

hydrophobic collapse

207
Q

T/F: proteins fold randomly

A

F

208
Q

Levinthal’s paradox

A

10^n conformations (n=# residues)

209
Q

T/F: proteins fold in seconds

A

T

210
Q

protein folding order

A
  1. formation of local segments of secondary structure during tsln right away
  2. hphobic collapse drives molten globule formation
  3. secondary structures are stabilized through long range interactions, driving tertiary structure formation
  4. rearrangements occur until final tertiary structure is acheived thorugh packing of internal side chains and formation of H bonds
211
Q

competetion btwn native state and ____

A

aggregation

212
Q

chaperones help proteins fold into

A

native state

213
Q

what does PDI do

A

mediates correct disulfide bridge formation via nuc attacks (PDI has own cysteine residues that initiate attack)

214
Q

molecular chaperones often recognize and bind ____ surfaces to block aggregation

A

hphobic

215
Q

T/F: most molecular chaperones do not require ATP hydrolysis for energy

A

F

216
Q

what happens with GroEL

A

1) unfolded protein is delivered to GroEL by HSP70 via ATP; hydrophobic patches bind unfolded substrates
2)ATP binds to GroEL and recruits GroES
3) cap binding causes conf. change that exposes the hydrophilic patches
4) protein can now re-fold in polar env
5) ATP is hydrolyzed and the cap and protein gets released

217
Q

protein misfolding can drive

A

alzheimer’s and prion disease

Biochem (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions