Protein Structure Flashcards

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1
Q

What are the two common covalent bonds between amino acids?

A

peptide bonds and disulfide bonds

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2
Q

What are peptide bonds?

A

link amino acids together in a polypeptide

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3
Q

What are disulfide bridges?

A

between thiols in cysteine R-groups

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4
Q

What is a peptide bond formed between?

A

carboxyl group of one amino acid to the alpha-amino group of another

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5
Q

What is the backbone of the polypeptide?

A

N-C-C-N-C-C pattern

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6
Q

What is an individual amino acid called in a polypeptide chain?

A

residue

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7
Q

Which terminus is always written first in a polypeptide? Which is written last?

A

first = amino-terminal
last = carboxy terminal

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8
Q

What is proteolysis?

A

hydrolysis of a protein by another protein

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9
Q

What is the enzyme that performs proteolysis?

A

protease or proteolytic enzyme

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10
Q

What role does a disulfide bridge play?

A

stabilizing the tertiary structure

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11
Q

What does it mean for a protein to be denatured?

A

disruption of a proteins shape without breaking peptide bonds

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12
Q

How can proteins be denatured?

A

urea, extreme temperatures, extreme pH, and changes in tonicity

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13
Q

What is primary structure of protein folding also known as?

A

sequence

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14
Q

What bond determines the primary structure of protein folding?

A

peptide bond

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15
Q

What determines the secondary structure of protein folding?

A

hydrogen bonds between the NH and CO backbones of polypeptides

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16
Q

What are the two motifs that can be formed during secondary structure of protein folding?

A

alpha helix
beta pleated sheet

17
Q

What is the tertiary structure of protein folding?

A

interactions of R-groups with each other and with the solvent

18
Q

What forces stabilize both tertiary and quaternary structure of protein folding?

A

van der Waals
hydrogen bonds
disulfide bonds
electrostatic interactions

19
Q

What is the quaternary structure of protein folding?

A

subunits interaction with other subunits