Three dimensional structure of proteins Flashcards

1
Q

At what wavelength do you measure proteins absorbance?

A

280 nm

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

At what wavelength do you measure DNA?

A

260 nm

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

What is needed to be able to measure absorbance of a protein?

A

Aromatic aa, mostly W but also Y and F.

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

What does fluoresence measure?

A

Stability and binding events

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

What does Far CD measure?

A

Secondary structure, can tell if a protein is folded or not

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

What does Near CD-measure?

A

Tertiary structure, proteins fingerprints

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

What is the perk with calorimetry?

A

It can be used with unpurified samples

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

What does ITC measure?

A

Ligand binding

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

What does DSC measure?

A

Unfolding of a protein

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

What does NMR measure?

A

Determines protein structure and changes in individual amino acids when binding a ligand

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

What does X-Ray do?

A

Determines protein structure of crystallized proteins

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

What does SPR measure?

A

Determines the dissociationg constant (Kd) by measuring the refractive index

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

What does identical residues mean when you are aligning two sequences from different species?

A

The compared spot in the sequence are the same residue

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

What does conserved substitution mean when you are aligning two sequences from different species?

A

The compared residues in the sequence have similar structure and the structure will therefor be similar. Not a drastic mutation

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

What does non-conservative changes mean when you are aligning two sequences from different species?

A

That the spot compared have significantly different aa, leading drastic change in structure

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

What is a ramachandran diagram used for?

A

The diagram is used to see if a secondary structure is likely to occur. Some residues are more likely to be eg an a-helix than others

17
Q

What does propensity mean?

A

The tendency of an aa to be in a certain secondary structure

18
Q

What does a propensity score above 1 indicate? And below 1?

A

> 1 => Prefered structure

< 1 => not a likely structure

19
Q

What does the ridges in grooves model mean?

A

It means that helicies often pack against each other matcher their grooves into another helix ridges

20
Q

How many residues does an a-helix have per turn?

A

3,6 residues

21
Q

How many residues does an 310 helix have per turn?

A

3

22
Q

How many residues does an pi-helix have per turn?

A

4,4

23
Q

How many residues does a (anti)-parallell b-strand have per turn?

A

2

24
Q

Where are 310 helicies found in proteins?

A
  • Regular a-helix is distorted by unfavorable residues
  • At the end of a regular helix
  • Short sequences in helical conformation