secondary structure of proteins Flashcards

1
Q

secondary protein structure

A

regular repetitive patterns in short sections of the polypeptide chain

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

polypeptide chain backbone

A

linked by C-C and C-H single bonds which are flexible due to bond rotation

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

Chain flexibility

A
  • arises from bond rotation not bond bending
  • single bonds allow for rotation about bond axis
    -normal 109 and 12- degree bond angles are present
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

conformations

A

state of molecule that can be interconverted by bond rotations without breaking covalent bonds
(different shapes of polypeptide chain)

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

configurations

A

can be interchanged by breaking covalent bonds, not by bond rotation
(cis and trans forms of a molecule)

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

X-ray diffraction

A
  • measures repeating patterns on molecular scale
  • measured in angstrom units
    1 Å= 1x10^-10 meter
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

resonance forms of the peptide bond

A

one with a C-N single bond and one with a C=N double bond
- peptide bond is rigid fixing in trans-geometry because it behaves more like a double bond than a single bond

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

rigid planes

A

alpha amino and carboxylate are locked in rigid planar peptide bonds and only 2 bonds to alpha carbon can rotate freely

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

restricted bond rotation

A

limits freedom of motion so only limited structures can form - 2 possible repeating patterns
1. helical shape - every alpha-carbon turns the same direction
2. extended shape - the alpha carbon turn in alternating directions

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

the alpha helix

A

forms when amino acids all have the same orientation and alpha-carbons turn same direction

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

the beta sheet

A

strands in the same direction make parallel b-sheet
- H-bonds connect strand to strand
strands in opposite directions make antiparallel b-sheet
- H-bonds align better in antiparallel mode

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

amino acids preferring beta configurations

A

W,Y,F,V,I,T,C
- these AAs are either large, have a branch or large S atom

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

amino acids preferring alpha configurations

A

M,F,L,K,H,A,R,E,Q
- this is the default behaviour of amino acids

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

what determines secondary structure form

A

local majority of amino acids that prefer alpha or beta

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

secondary structure breakers

A

G,P,N,D,S
- disrupts secondary structure by forming a turn or loop allowing polypeptide chain to change direction up to 180 degrees
- 2 breakers in a group of 4 amino acids interrupts the secondary structure

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