Lecture 7 - Protein Folding Flashcards

0
Q

Name the charged amino acids that can have ionic interactions

A
Aspartate (-)
Glutamate (-)
Arginine (+)
Lysine (+)
Histidine (+)
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1
Q

Name the polar amino acids that can hydrogen bond

A

Serine
Threonine
Asparagine
Glutamine

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2
Q

Name the nonpolar amino acids that can have hydrophobic interactions

A
Alanine
Valine
Leucine
Isoleucine
Methionine
Tryptophan 
Phenylalanine
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3
Q

What kind of interactions operate over short distances?

A

Van der Waals interactions

Attractive force is proportional to (distance)^-6

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4
Q

True or false? Van der Waals interactions results from the overlap of long-lived highly fluctuating dipoles of non-bonding electron orbitals

A

FALSE.

Short-lived

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5
Q

True or false? Inside the densely packed protein interior, numerous van der Waals interactions sum up and contribute to the stability of a folded protein

A

True

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6
Q

What facilitates dance packing in van der Waals interactions?

A

Availability of hydrophobic side chains (R groups) of many shapes and sizes

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7
Q

What kind of interaction explains why seemingly conservative substitutions of one hydrophobic side chain with another can greatly affect protein stability

A

Van der Waals

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8
Q

True or false? Protein folding increases interactions between the protein and water.

A

FALSE.

decreases not increases

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9
Q

True or false? Hydrogen bonding is a driving force for protein folding because H-bonds with water are broken to make intramolecular H bonds

A

FALSE

It is NOT a driving force

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10
Q

True or false? H bonding changes did not affect free energy much.

A

TRUE, because the formation of extended H bond networks (especially in α-helices or β-sheets) compensate for loss of AA-water bonds

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11
Q

What kind of interaction is a major contributor into protein folding and stability?

A

Hydrophobic interactions

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12
Q

True or false? Proteins fold with hydrophobic residues on the interior.

A

True

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13
Q

Does protein folding increase or decrease the entropy of the protein water system?

A

Protein folding increases entropy of the protein-water system because water is less ordered (ΔS is positive)

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14
Q

Once a protein folds, the protein structure can be stabilized by the formation of what kind of bond?

A

Disulfide bonds (-S-S-) between sulfhydryls (-SH) of cysteine

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15
Q

What is the -S-S- covalent bond energy?

A

200-800 kJ/mol

16
Q

What denatures or unfolds proteins?

A

Organic solvents, urea, detergents, and heat

17
Q

True or false? Some proteins can spontaneously refold into native 3-D structure

A

True

18
Q

True or false? Ribonuclease A can be denatured and renatured.

A

True

19
Q

Formation of some secondary structures (α-helices and β-sheets) leading to an intermediate structure

A

Nucleation

20
Q

Name the status of protein folding in model one

A

Nucleation, structural consolidation to form intermediate state, final rearrangements

21
Q

Continued formation of secondary structure and beginnings of tertiary structure to give higher level intermediate structures

A

Structural consolidation to form intermediate states

22
Q

All basic elements in place and final adjustments for a fully functional protein. What stage of protein folding?

A

Final rearrangements state

23
Q

How does protein folding occur according to the second model?

A

Formation of compact state due to hydrophobic interactions.
Compact state called “molten globule”
Structure grows out of this collapsed state

24
Q

Helper proteins that assist polypeptide folding into native structure (or prevent improper folding or aggregation)

A

Chaperonins

25
Q

Example of a molecular chaperone

A

GroEL-GroES complex

26
Q

What is spongiform encephalopathy also known as?

A

Mad cows disease

27
Q

Where is prion found?

A

In the central nervous system