3D, primary and secondary Flashcards

1
Q

what kind of double bond do peptide bonds feature and why

A

partial double bond due to resonance

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

describe the length of the C=O bond in a peptide bond

A

longer than usual

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

describe the length of the C-N bond in a peptide bond

A

shorter than usual

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what configuration are most peptide bonds in in proteins

A

trans

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

which bonds can rotate in an polypeptide

A

the ones attached to alpha carbons only, phi and psi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

which atoms define torsion

A

central 2 and the 2 on either side

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

draw trans 180 newman conformations for phi and psi

A

see slide 13

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

why is L-proline restricted in rotation? which bond is this around?

A

phi bond restricted because cyclic side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what kind of bonds are found in regular secondary structure?

A

repeating phi and psi angles for sequential amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what kind of H-bonding patterns do stable forms of secondary structures feature?

A

repeating

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what are 3 examples of regular secondary structure

A

alpha helix, beta sheets, collagen helixes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what kind of bonds are found in irregular secondary structures

A

non repeating phi and psi angles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what are 3 types of irregular secondary structure

A

beta turns, coils, loops

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what kind of twist is in the alpha helix

A

right handed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

where are the H-bonds in an alpha helix

A

c=o of i and NH of i+4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

where do the sidechains project in an alpha helix

A

away from core

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what is the bond angle for phi and psi in an alpha helix

18
Q

how many residues per turn of alpha helix

19
Q

which R-groups from the primary sequence interact favourable in alpha helix

A

3-4 residues apart

20
Q

what are atoms in the alpha helix backbone stabilized by

A

van der waals and H-bonding

21
Q

which terminus in the alpha helix is negatively charged

A

C-terminus

22
Q

which terminus in the alpha helix is positively charged

A

N-terminus

23
Q

which direction is the C=O bonds pointing towards in an alpha helix

A

C-terminus

24
Q

what is found at each end of the alpha helix

A

4 unpaired amino acids not involved in H-bonds

25
which amino acids are usually found ar the N-terminus of an alpha helix? what about the C-terminus
glu and asp lys and arg
26
which end of an amino acid would interact with phosphates or nucleotides
the N terminus
27
what are the 3 kind of beta sheets
parallel antiparallel mixed
28
what is phi and psi for parallel beta sheets what is phi and psi for antiparallel beta sheets
(-120, +120) (-140, +140)
29
what are beta sheets formed by
H-bonds between strands
30
what are the 2 types of situations involving strands for beta sheets
separated within primary structure or coming from different peptides
31
compare the repeat period for parallel vs antiparallel beta sheets
shorter for parallel
32
T or F: the hydrogen bonding pattern for antiparallel vs parallel beta sheets is the same
false
33
T or F: individuals strands in a beta-sheet always follow each other in the primary sequence
false
34
are beta sheets planar
no they are not planar
35
what can beta sheets twist into
saddle shapes or barrels
36
where are the H-bonds between in beta turns
C=O of residue 1 to NH of residue 4
37
what is the degree change in the direction of the polypeptide in a beta turn
180 degrees
38
how are the types of beta turns characterized
combinations of phi and psi angles
39
which amino acids are often found in beta turns
proline and glycine
40
what is always the third residue in a type II beta-turn? why is this? what is the name/ designation for this third residue?
glycine geometry (80,0) i+2
41
which amino acids have the highest propensity for alpha helix formation
ala glu and met