3.3 Proteins Flashcards

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1
Q

What are the four levels of protein structure?

A

1, 2, 3, and 4 degrees

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2
Q

What is the 1 degree of protein structure?

A

primary structure

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3
Q

What is the 2 degree of protein structure?

A

secondary structure

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4
Q

What is the 3 degree of protein structure?

A

tertiary structure

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5
Q

What is the 4 degree of protein structure?

A

quaternary structure

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6
Q

What happens during protein denaturation?

A

this is the unfolding of a protein that destroys functionality, they disrupt hydrogen and ionic bonds. some can return back to their original structure but most of the time they cannot

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7
Q

How is tertiary structure formed by hydrophobic interactions?

A

hydrophobic groups cluster together on the inside of the protein leaving hydrophilic amino acids on the outside to interact with surrounding water molecules

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8
Q

How is tertiary structure formed by hydrophilic interactions?

A

it is stabilized by the outside polar hydrophilic hydrogen and ionic bond interactions

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9
Q

How is tertiary structure formed by acidic and basic side chains?

A

the particular proteins determine its tertiary structure

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10
Q

How is tertiary structure formed by cysteine side chains?

A

they act like molecular safety pins, keeping parts of the polypeptide firmly attached to one another

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11
Q

Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?

A

The structure would change because the protein would not be able to bend and go into the correct shape it needs to. If the structure changes, then it won’t be able to carry out its proper function, it won’t be able to do anything.

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