Protein Folding and Unfolding Flashcards Preview

BMS I > Protein Folding and Unfolding > Flashcards

Flashcards in Protein Folding and Unfolding Deck (30)
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1
Q

Pauling

A

alpha and beta is enough to fold-all from one polymer

2
Q

Anfinsen

A

all needed to fold is in polypeptide sequence

3
Q

Levinthals

A

some sort of process that drives folding preferred way

4
Q

A4- principal of minimum frustration

A

amino acids position themselves in way to do folding

5
Q

Why can’t all proteins self fold

A

locailzed high energy transition state

6
Q

groEL chaperone

A

conserved across evolution

7
Q

protein repair vs deg

A

try repair numerous times, then degrade

8
Q

chaperone abilities

A

matchmaker, trafficker, quality control, protein disassembly, molecular CPR, complex assembly (subunits in proper place)

9
Q

chaperone role during protein syn

A

guide during folding (much done by RNA itself however), protect nascent dna, avoid kinetic dead ends

10
Q

cotranslational protein degradation

A

irreversibly damaged protein brought immediately from synthesis site to protease

11
Q

proteosome strcuture

A

four rings, outer are identical (alpha subunit), inner are identical, hydrolytic activity (beta unit)

12
Q

UMP1

A

chaperone for proteasome synthesis, first target of proteasome

13
Q

interactions that impact folding

A

hydrophobic core, electrostatic, VDW forces, disulfide bonds, metal coordination

14
Q

Molten globule+final 2 steps

A

Almost completely folded-hydrophobic collapse and water exclusion

15
Q

Hierarchical, nucleation, and hydrophobic collapse protein folding models

A

Secondary structures form first then combine, cascade, obvious

16
Q

disulfide bond

A

even if things are cut one way-as long as held close together (by disulfide bond in this case) can re attach

17
Q

RING Motif

A

Zinc coordation domain, coordinates metal atom which traps conformation in many TFs

18
Q

Agents that promote unfolding

A

Temp, pH, Urea, pressure, guanidine, organic solvents

19
Q

Fold to tertiary or quaternary proteins (in sequence)

A

Use chaperones to not immediately bind with proximal protein-instead move on to tertiary/quat

20
Q

Isomerase chaperones

A

Clip protein and reform

21
Q

ERAD

A

Endoplasmic retiduclum assocated degradation

  1. Ribo and chap dock onto ER membrane (send in unfolded=presence of ER chaperones)
  2. Something doesn’t work out-send unfolded protein back out way it came in
  3. Proteasome waiting at other end of tunnel
22
Q

CFTR Delta 508

A

Protein folds extremely slowly-protease destroys before full folding complete

23
Q

Protein aggregation

A

Common cause of many neurodegen diseases (ex Parkinsons/Huntingtons)

24
Q

chaperone and protease

A

very similar structure (non polar barrel in both) also subunit congruency is the same

25
Q

Key features of chaperone

A

not all need ATP, leave after doing job

26
Q

Important determinants for protein folding

A

hydrophobic core, electrostatic, VDW forces, disulfide bonds, metal coordination

27
Q

Sig of water exclusion

A

hydrophobic collapse results in very close but not final-then water exlcuion is final driving force in folding

28
Q

Biochem activités that require chaperones

A

3 main-assembling large complex, secretion, repairing damaged but many more

29
Q

Different forces that stabilize native protein structure

A

Hierarchical , Nucleation/Condensation, Hydrophobic Collapse

30
Q

Proteasome/rearrageing scaffolding mech

A

bind with non polar residues, use 7 ATP, shift non polar residues away pulling apart molecule