Protein Structure Flashcards

1
Q

phi dihedral angle

A

N-C(a)

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2
Q

psi dihedral angle

A

C(a)-C

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3
Q

omega dihedral angle

A

C-N
cannot freely rotate due to partial double bond character

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4
Q

99% of residues in a protein are what conformation?

A

trans

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5
Q

pitch

A

5.4 ang
vertical distance between conseuctive turns of the helix

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6
Q

which residue is cis

A

proline

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7
Q

n

A

number of residues (3.6)

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8
Q

d

A

distance between residues
1.5 Ang

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9
Q

p =

A

n times d

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10
Q

dimension of backbone

A

5-6 Ang

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11
Q

backbone carbonyl of amino acid i forms ___ bond with

A

h bond with amine of i+4

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12
Q

3 10 helix

A

i and i +3, more tightly would

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13
Q

pi helix

A

i and i + 5, less tightly wound

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14
Q

distance between residues in beta pleated sheet

A

7 angstrom

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15
Q

are h bonds weaker in parallel or antiparallel beta pleated sheets

A

parallel

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16
Q

coiled coil held together by

A

nonpolar interactions btwn strands

17
Q

every 3-4 AA in keratin is hydrophobic so

A

strip of contiguous hydrophobic surface area along
one face of each helical chain

18
Q

alpha keratin has a high level of

19
Q

alpha keratin can be hardened by

A

introduction of disulfide cross-links within the several
levels of fiber structure

20
Q

in fibrion, almost every other residue is _____ followed by

A

glycine, serine or alanine

21
Q

every third residue in triple helical cable (collagen) is

22
Q

in collage triple helical cable, ___ bonds between backbone_____ and ______ protons hold chains together

A

H-bonds, carbonyls, amide

23
Q

in collagen truple helical cable, _________ are packed at the interface of the helical bundle

24
Q

enzyme necessary to catalyze proline –> hydroxyproline

A

ascorbic acid

25
what group of hydroxyproline seems to participate in stabilizing the protein (collagen)
OH
26
cross linking of collagen molecules require
lysine side chains
27
AA commonly found in beta turns
glycine + proline
28
the coiled coil is ____ handed
left
29
most alpha-helices are ______ handed
right
30
fibrion protein sequence
Gly - ala/ser - ala/ser
31
collagen protein sequence
Gly - proline - hydroxyproline
32
proteins are very insoluble at
pI