Chapter 4 Flashcards

1
Q

average molecular weight of an amino acid

A

110

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

How do you approximate the number of amino acids in a protein?

A

dividing the proteins molecular weight by 110.

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

smallest protein

A

insulin: ~50

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

biggest protein

A

titin

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

The 3D structure of a protein is determined by…

A

its amino acid sequence

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

the most important forces stabilizing the specific structures of a given protein are…

A

non-covalent

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

low free energy means…

A

most stable

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

Folded proteins occupy a….

A

low-energy state

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

Protein folding _________ the order.

A

increases

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

denaturation

A

loss of activity; reversible (energy required is small)

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

Folding and unfolding is a ______________ process

A

cooperative

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

cooperative process

A

as soon as some come apart, it all comes apart

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

Within main-chain of the polypeptide, there is a repeating pattern of…

A

NCCNCC

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

To represent a viable form of secondary structure, the folding pattern must:

A
  • optimize the hydrogen bonding potential of main chain carbonyl and amide groups
  • represent a favoured conformation of the polypeptide chain
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

There are _____ numbers of hydrogen bond donors and accepts within the polypeptide main chain.

A

equal

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

most residues within biological peptides and proteins tend to be in….

A

trans configuration

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

Trans configuration can’t convert to cis without….

A

breaking bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Each alpha carbon is held within the main chain through…

A

single bonds with complete freedom of rotation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Phi

A

alpha carbon to amide nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Psi

A

alpha carbon to carbonyl carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Ramachadran Plot

A

Illustrates all possible combos of Phi and Psi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

alpha helices are ______ handed helices

23
Q

right handed helix

A

3.6 residues/turn

24
Q

alpha helices are stabilized by..

A

many hydrogen bonds which are parallel to helix axis

25
All C=O groups point towards....
C-terminus
26
Which amino acids are usually not found in alpha helices?
proline and glycine
27
Stretches of similarly charged residues will ________ alpha helices due to ______________.
destabilize, electrostatic repulsion
28
The positioning of hydrophobic and hydrophilic residues with primary structure generates.....
an amphipathic alpha helices
29
conformation of beta strands
- fully extended polypeptide chains | - side chains projected alternately above and below
30
How are beta strands stabilized ?
by hydrogen bonds between C=O and -NH on adjacent strands
31
Which are more stable, parallel or anti-parallel beta sheets?
anti
32
Unique _______ produced at the interfaces between subunits of quaternary structure.
active sites
33
Keratin primary structure
-pseudo seven repeat (a and d are hydrophobic)
34
Keratin secondary
right handed, amphipathic alpha helices
35
keratin tertiary
the hydrophobic strip in alpha helical rods are looking for hydrophobic environment
36
keratin quaternary structure
hydrophobic surfaces interact to form coiled coils
37
coiled coil of keratin
-two right-handed helices wrapping in a left-handed fashion
38
Individual units of keratin are linked together through...
disulfide bonds
39
What determines overall strength of keratin?
extent of disulfide bonds
40
collagen makes up...
tendons, skin
41
collagen primary
multiple repeats of Gly-X-Y where X is often proline or hydroxyproline
42
collagen secondary
-formations of left handed helices (3 residues/turn)
43
collagen tertiary
full length helical
44
quaternary
coiled coils
45
coiled coils of collagen
three left handed helices wrapping in right handed fashion
46
What determines strength of collagen?
linkages from amino acid residues that undergo post-translational modification
47
The enzyme that performs performs the stabilizing links (involving p.t.m residues) of collagen require....
VITAMIN C
48
silk primary
six residue repeat (GSGAGA)
49
silk secondary
composed primarily from beta sheets (strength)
50
silk is both flexible and strong because...
- fully extended polypeptide chains (strength) - beta sheets (flex) - association of sheets by van der Waals and hydrophobic interactions (flex)
51
Hydrogen bonds hold....
beta sheets together (non-covalent)
52
hydrophobic and van der Waal interactions bring ________ together
beta sheets
53
Entire helix is a dipole with N (__) and C (__).
N=+ | C= -