Chapter 5- Secondary Structure Flashcards

1
Q

Primary structure definition

A

amino acid sequence of protein

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

Secondary structure definition

A

local spatial arrangements of the backbone atoms

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

Tertiary structure definition

A

3D structure of the entire polypeptide chain

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

Quaternary structure definition

A

Spatial arrangements of protein subunits

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

Peptide bonds are ____ bonds

A

amide bonds

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

Proteins result from the formation of covalent peptide bonds by

A

Condensation

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

A polymer of two amino acids is called

A

dipeptide

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

A polymer of many amino acids

A

polypeptide

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

Avg mass of amino acid

A

110 g/mol

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

Polypeptides are _____ polymers not branched

A

linear

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

The alpha H bonds and carboxyl groups run in the _____ direction

A

same

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

Amino acids are always read from the __ terminus to the __ terminus

A

N (amino terminus), C

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

In a peptide group a C–N bond is ___ than a simple amine, while a C=O bond is ____ than a simple ketone

A

Shorter, Longer

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

Peptide bond has _____ double bond character

A

~40%

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

C–N torsion angle is called __ and the C–C torsion angle is called ___

A

Phi, Psi

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

The trans configuration is more favored than the cis configuration because

A

the trans configuration has less steric hindrance and is more stable

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

the C–N bond is unable to ____

A

Rotate

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

Side chains dictate the bond angles because

A

different bond angles reorient to accommodate other groups around it

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

An alpha helix can be right-handed or left-handed which means it has

A

Chirality

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

Glycine in a peptide chain provides

A
  • flexibility to proteins
  • often found in places where proteins make sharp turns
16
Q

Proline in a protein chain provides

A
  • structure rigidity (due to cyclic side chain)
  • may be found in kinks of the protein
17
Q

polypeptide made of L-alpha amino acids will have n=___ and pitch =____

A

3.6 amino acids per turn, 5.4 A

18
Q

____ and _____ of peptide bond point along the long axis (in the opposite direction)

19
Q

The sum of all H bonds contributes to stability which means

A

more H bonds= more stability

20
side chains in an alpha helix point
outwards (avoids steric interference)
21
How do side chains affect stability?
1. affecting the peptide backbone 2. through side chain- side chain interactions
22
How many degrees between each amino acid in an alpha helix
100
23
interactions between side chains can lead to either the ______ or _______ of the helix
destabilization or stabilization
24
Steric clash means
two large bulky side chains stacked on top of each other is more likely to destabilize the helix
25
ASP and LYS have formed a _____ interaction
salt bridge that stabilizes the helix (different charges)
26
Asp and Glu have a _____ interaction
repulsion interaction that destabilizes the helix (same charges)
27
Aromatic amino acids can ____ which are favorable ______ ________
stack ( pi stacking), hydrophobic interactions
28
amino acids that tend to form an alpha helix
MALEK (met, ala, leu, glu, and lys)
29
Beta-branched amino acids that make them more difficult to adopt an alpha-helical conformation
Val, Ile, Thr
30
Amino acid that is entropically expensive and destabilizes helices
Gly
31
Conformationally rigid with no H bonding possible, known to destabilize helicies and may form a kink
pro
32
All dipoles in an alpha helix point in the ____ direction which results in a ______ ______ between the C terminal and N terminal
same, macro dipole (c end is neg and N end is pos)
33
Dipoles in an alpha helix result in
destabilization through entropic effects
34
the N terminal of an alpha helix is often capped by a _____ side chain while a ____ side chain caps a C terminal
negative, positive
35
Antiparallel beta sheets involve two chains running in ____ directions, the H bonds are ~ ______ to each other
opposite, parallel
36
Parallel beta-sheets involve two side chains running in the _____ directions, the H bonds are formed on ____
same, angles
37
Beta strands exhibit a _____ ______ ______ due to the chirality of the amino acids
right-handed twist
38
Beta turns are commonly formed by
proline and glycine
39
beta turns give proteins _____ and promotes the formation of _______ ______ ____
globularity, anti-parallel beta sheets
40
The coil/loop conformation is completely ______ and is typically found on the _____ _____ of the proteins
unstructured, outer surface
41
Random coils are usually ______ and ______ but do not conform to any ______ ______ ____
organized and stable, frequently recurring pattern
42
The stability of seconds structures is determined by
1. steric repulsion minimized 2. H bonding is maximized
43
Characteristics of Circular Dichroism Spectroscopy
- absorption spectroscopy - provides information on the secondary structure content of proteins - signal; originated from the amide group and the phi/ psi angles