4.3 Secondary Structure of Proteins Flashcards

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1
Q

What 2 bonds have free rotation w/in each aa

A

1) bond btwn alpha carbon and amino nitrogen of that residue

2) bond btwn alpha carbon and carboxyl group of that residue

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2
Q

is the peptide group planar

A

yes

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3
Q

the angle phi is used to designate which rotation

A

C-N bonds

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4
Q

the angle psi is used to designate which rotation

A

C-C bonds

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5
Q

What are some periodic secondary structure

A

alpha helix and beta pleated sheets

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6
Q

How is the helical conformation very stable?

A

stabalized by H2 bonds paprallel to the helix axis w/in the backbone of single poptide chain, from N-terminal, C-0 group of each aa residue is H2 bonded to N-H group of the aa four residues away from it in the covalently bonded sequence. helical conformation gives bonds max strength, linear arrangement

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7
Q

How many residues for each turn of the helix

A

3.6 residues

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8
Q

What can disrupt the alpha helix

A

proline by creating a bend in the backbone b/c its cyclic structure

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9
Q

Why can’t proline fit into the alpha helix

A

rotation around the bond btwn the N and aloha carbon is restricted, proline’s amino group cannot participate in intrachain H bonding

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10
Q

What other localized factors can disrupt alpha helix

A

strong electrostatic repulsion owing to proximity of several charged groups of same sign, cowding (steric repulsion) caused by proximity of bulky side chains

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11
Q

in the alpha helical conformation where do sides lie

A

all lie outside the helix and crowing can occur if it is bonded to 2 atoms other than hydrogen (VAL, ISO, THR)

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12
Q

How is B-pleated sheet diff than a-helix

A

peptide backbone in b-sheet is almost completely extended. H2 bonds are perpendicular ot directn of protein chain, not parallel like alpha helix

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13
Q

when are beta sheets parallel

A

if the peptide chains run in smae direction (if they are aligned in termed of their N and C terminal end)

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14
Q

When are antiparallel pleated sheets formed

A

when alternating chains run in opposite directions

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15
Q

what gives rise to the name pleated sheets

A

H2 bonding btwn peptide chains in beta-pleated sheets give rise to a repeated zigzag structure

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16
Q

how are hydrogen bonds diff from ones in alpha helix

A

H2 bonds are perpendicular to direction of protein chain not parallel as in alpha helix

17
Q

How are super secondary structures in proteins form

A

combination of alpha and beta strands combined in many ways

18
Q

Describe the beta alpha beta unit

A

two parallel strands of beta sheets are connected by a stretch of alpha helix. Less stable than anti parallel

19
Q

Describe the alpha alpha (helix-turn-helix) unit

A

consists of 2 antiparallel alpha helices

20
Q

Where is energetically favorable contacts in helix-turn-helix

A

energetically favourable contacts exists btwn the side chains in the 2 stretchs of helix

21
Q

What is a beta meander

A

an antiparallel sheet formed by a series of tight reverse turns connecting stretches of the polypeptide chain

22
Q

what is a greek key

A

antiparallel sheet formed when polypeptide chain double nack on itself in a pattern similar to a decorative design from classical period

23
Q

What is a motif

A

a repetitive supersecondary structure

24
Q

what is collagen

A

a component of bone and connective tissue, most abundant in vetebrates. organized in water-insoluble fibers

25
Q

What is a collagen fiber consist of

A

3 polypeptide chains wrapped around each other in a ropelike twist or triple helix

26
Q

describe the 3 chains of collagen

A

each of 3 chains had a repeating sequence of 3 aa residues X-PRO-GLY or X-HYP-GLY (hyp-hydroxyproline)

27
Q

What is hair pin super secondary structure

A

Anti parallel beta sheets

28
Q

What are tim barrels

A

Beta barrels comprised of alternating beta alpha beta units. Seen in private kinase