4 Flashcards

1
Q

how is hemogolbin described

A

tetramer or dimer of alpha-beta protomers

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2
Q

what feature makes a structure an oligomer

A

repeating units

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3
Q

what is the repeating unit in an oligomer

A

protomer

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4
Q

what are oligomers associated with

A

a symmetry form

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5
Q

how are errors in translations affected by the quaternary structure

A

less critical

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6
Q

what is pseudosymmetry

A

non-identical homologous subunits are related by symmetry

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7
Q

what are the types of symmetry

A

Cyclic, dihdedral, tetrahedral, octahederal, isocaheadral

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8
Q

describe the axes in Dn

A

2N protomers arranged around 2 axes
one N fold and one 2 fold

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9
Q

what is helical symmetry

A

protomers related by rotation and translation

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10
Q

what are the fold axes in tetrahedral symmetry

A

3 fold and 2 fold

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11
Q

what are the fold axes in octahedreal symmetry

A

2, 3, 4

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12
Q

what are the fold axes in icosahedral

A

2, 3, 5

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13
Q

what are the types of forces in protein folding

A

weak, non covalent

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14
Q

what can destroy the native state of a protein (4)

A

heat pH detergents organic solvents

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15
Q

what are the two denaturants of interest

A

guanidinium and urea

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16
Q

descibe the effects of the two denaturants of interest

A

chaotropic, water soluble, disrupt H-bonding

17
Q

what are the two reducing agents of interest

A

beta-mercaptoethanol and DTT (dithiothreitol)

18
Q

what kind of process is denaturation

A

cooperative

19
Q

what is the midpoint of transition for denaturant characteristic of

A

protein and denaturant

20
Q

what effect does unfolding part of the protein have on the energy required to unfold the rest of the structure

21
Q

what is the state between secondary and tertiary structure

A

molten globule

22
Q

what is misfolding

A

stable structure but not native

23
Q

what are the disease states leading to misfolding

A

amyloidosis - huntington’s / alzeimers
prion disease - BSE, scrapie
collagen defects - osteogenesis imperfecta

24
Q

what 2 things can assist with folding

A

chaperones or isomerases

25
what are the 2 types of molecular chaperones
chaperonins and Hsp
26
what sre the two types of isomerases
protein disulphide isomerase peptide prolyl isomerase
27
how do chaperones work
isolate misfolded proteins so they do not interadr
28
what do chaperones use to carry out their activity and why
energy (ATP hydrolysis) to unfold the protein substrate
29
is chaperone activity kinetic or thermodynamic
kinetic
30
what are the two bacterial chaperones of interest
DnaK Hsp70 and DnaJ Hsp40
31
what is responsible for the nucleotide exchange associated with protein assisted folding
GrpE
32
what does ATP hydrolysis do for assisted folding
changes binding site for protein substrate
33
describe Hsp 70 and Hsp 40 actions
DnaK binds with ATP then associates with DnaJ and midfolded substrate
34
what is the GroEL/GroES complex (chaperonin)
1. GroES cap binds to GroEL ring 2. unfolding of misfolded protein with ATP hydrolysis (7 ATP) 3. another misfolded substrate enters with 7 ATP 4. release of GroES cap, ADP and protein
35
what are the two properties of PDI
isomerase or oxidoreducatase