Secondary, tertiary and quaternary structures (Dr.Miles TAMU) Flashcards

1
Q

Hydrogen bonds in proteins structure

A

the components the peptide backbone tend to form H-bonds with one another. Each hydrogen will contribute 12kJ/mol of stabilization energy

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

Hydrophobic Interactions in proteins structure

A

This clustering in entropy driven and will also cluster in nonpolar environments
- almost al side chains are nonpolar

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

Electrostatic Interactions in proteins structure

A

Almost always located on the surface of the protein and interact with the solvent water molecules and salts

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

Dipole-Induced Dipole Interactions in proteins structure

A

accounts for 0.1-4 Kj/mol of stabilization

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

What amino acid can have both cis and trans with steric strain

A

Proline

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

Psi bond location

A

rotation around Ca-C bond

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

phi Bond location

A

Rotation around Cn-C bond

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

Alpha-helix residues n and p

A

n= 3.6
p= 5.4

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

what are the 5 constraints that effect stability

A

1.) Electrostatic repulsion or attraction of successive amino acid residues with charged side chains destabilize the alpha Helix.
2.) Successive bulky amino acids destabilize the alpha Helix.
3.) The interactions of amino acids spaced three residues apart have a great effect the stability of the
alpha Helix.
4.) The occurrence of proline or glycine residues destabilizes the helix.
- Proline is cyclic and rigid.
- It produces a kink in the helix. The alpha amino nitrogen atom is part of the rigid ring and
cannot participate in the back bone hydrogen bonding.
- Glycine has too much conformational flexibility.
5.) The interaction between amino acid residues at, the ends of the helix that interact with the dipole
moment inherent of the alphahelix effect the stability of the helix.
- Negatively charged amino acids at the N-terminal stabilize the helix. Positively charged
amino acids at the C-terminal end stabilize the helix by charge-dipole interactions.
The

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

3^10 helix n and p

A

n=3
p=6

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

Antiparallel beta pleated sheet n and p, and what is is

A

n=2
p=7
Is the fundamental structure of silk and is completely streached

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

Parallel beta sheets n and p

A

n=2
p= 6.5

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