Tertiary structure of fibrous proteins Flashcards

1
Q

what secondary structure dominates the structure of fibroin

A

beta sheets

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2
Q

what are alpha-keratins enriched for

A

cysteine and alanine

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3
Q

what are the structures of alpha-keratins reinforced by ?

A

disulfides

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4
Q

what does “harder: refer to in a keratin structure?

A

more disulfides

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5
Q

what are the 2 chains in a dimer twisted into in an alpha ketain

A

left-handed coiled coil

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6
Q

what percent of protein mass in mammals is collagen

A

25-35%

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7
Q

where is collagen found

A

skin bones teeth

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8
Q

what is collagen composed of? (in terms of structure)

A

regular, helical structure

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9
Q

what is tthe handedness of collagen

A

left handed

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10
Q

how many residues per turn of collagen

A

3

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11
Q

what do 3 collagen chains assemble into

A

right handed super helix

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12
Q

what is the primary structure of collagen characterized by?

A

glycine-proline-hydroxyproline

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13
Q

where does hydrogen bonding occur in collagen

A

between strands, not within them

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14
Q

what are collagen chains rich in?

A

glycine, proline, 4-hydroxyproline, 5-hydroxylyysine

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15
Q

when does hydroxylation of 4-hydroxyproline occur?

A

after protein synthesis

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16
Q

what is required in the reaction of forming 4-hydroxyproline

A

ascorbic acid (vitamin c)

17
Q

where does 5-hydrxoylysine appear in collagen

A

intervals

18
Q

what is required in the formation of 5-hydroxylysine?

A

vit c

19
Q

how does cross-linking occur in collagen?

A

lysine, hydroxylysine, and histidine

20
Q

what is consistent to all soluble globular proteins?`

A

mixtures of secondary structure + irregular
hydrophobic cores
closely packed interior
maximum H-bonds in the interior

21
Q

what are the differences between different soluble globular proteins

A

secondary structure composition
prosthetic groups
disulfide presence

22
Q

where does extensive H-bonding occur in soluble globular proteins

A

within not between

23
Q

what is the handedness of connections between beta strands in soluble globular proteins

A

right handed

24
Q

what is conserved better, structure or sequence?

A

structure

25
Q

what are supersecondary structures

A

motifs and domains

26
Q

what are motifs

A

recognizable combinations of secondary structure that appear in a number of different proteins

27
Q

what are domains

A

discrete, independently folded compact units within a polypeptide

28
Q

can domains include motifs?

A

yes

29
Q

what are two motifs that satisfy hydrophobic burial

A

betaalphabeta or alphaalpha

30
Q

what is the complex motif made from the b-a-b loop motif

A

alpha/beta barrel

31
Q

what is a leucine zipper

A

coiled coil containing two alpha with leucines in the helix:helix interface

32
Q

what is the handedness of a leucine zipper

A

left handed superhelix