Protein Folding Flashcards

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1
Q

How does entropy play into protein folding?

A

Increases in entropy= favorable, and a decrease in entropy is unfavorable. Folding is favorable because the entropy of the surroundings become more disordered!

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2
Q

T or F:Solvation layers form around all solutes in solution.

A

T

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3
Q

True or false: If an unfolded protein causes a solvation layer to form around the protein, then the folded form of the protein will also result in a solvation layer.

A

True

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4
Q

Denaturation

A

Loss of all structures except primary

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5
Q

How do pH denaturants impact structure?

A

They disrupt charge based interactions

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6
Q

How do detergents impact structure?

A

they are amphitathic, they can disrupt hydrophobic interactions. SDS is a detergent

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7
Q

How do reducing agents impact strucutre?

A

Disrupt covalent bonds so it would disrupt disulfide bridges

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8
Q

How does urea impact structure?

A

it impacts H bonds

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9
Q

How does temp impact protein function?

A

Extreme temperatures disrupt protein function in different ways. High temperatures disrupt secondary, tertiary, and quaternary structure, denaturing the protein. Lower temperatures decrease the interaction between protein and substrate because of the decreased molecular collisions.

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10
Q

T or F: salt bridges would be disrupted by changes in pH

A

True. Salt bridges form between oppositely charged ionic side chains. Altering the pH can change the charges that these ionic side chains carry, which can disrupt the ionic interactions.

C

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