Protein Structure Flashcards

1
Q

What are amino acids linked together by?

A

Peptide Bonds

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2
Q

Primary

A

the linear sequence of amino acids in a protein

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3
Q

Secondary

A

the local 3-dimensional structure of the peptide backbone

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3
Q

Tertiary

A

the global arrangement of secondary structure, amino acid R groups and prosthetic groups

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4
Q

Quaternary

A

the arrangement of multiple protein molecules in complexes

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5
Q

N-Terminal

A

Amino Terminal

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6
Q

C-Terminal

A

Carboxyl Terminal

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7
Q

What form the peptide “backbone” of proteins?

A

Atoms of the peptide bonds and alpha-carbnos

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8
Q

Primary structure ______ all other levels of structure

A

dictates

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9
Q

What are the 4 major classes of secondary structure?

A

Alpha Helix, Beta sheet, turns, and random coil

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10
Q

Alpha Helix

A

a helical region of the peptide backbone that is stabilized by hydrogen bonding within the helix

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11
Q

Where are R groups in alpha helices?

A

Sticking outward

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12
Q

Beta Sheet

A

a planar arrangement of several peptide backbones that is stabilized by hydrogen bonding to adjacent beta strands

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13
Q

Where are R groups in beta sheets?

A

Sticking up and down from the beta sheets

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14
Q

In beta sheets, adjacent chains can be _____ or ______.

A

parallel; antiparallel

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15
Q

What structure interacts to give a protein its tertiary structure?

A

Secondary

16
Q

What can portions oof tertiary structure define?

A

Domains

17
Q

What energy state are the proteins in their native fold?

A

Low energy state

18
Q

Are proteins rigid once folded?

A

No

19
Q

Homodimers

A

Dimers formed between identical polypeptide monomers

20
Q

Heterodimers

A

Dimers between different polypeptide monomers

21
Q

Denature

A

Protein unfolding/uncoiling

22
Q

Is primary structure maintained in protein denaturing?

A

Yes

23
Q

What does protein denaturation do?

A

Eliminates enzyme function

24
Q

Is denaturation reversible?

A

In some cases, but usually is irreversable

25
Q

What was Anfinsen’s experiment?

A

a dialysis experiment to demonstrate that he could renature a protein after it was denatured