User:Eric Martz/Ramachandran Principle Quiz

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- A limited range of psi angles with all possible phi angles.
- A limited range of psi angles with all possible phi angles.
||See [[Protein primary, secondary, tertiary and quaternary structure]].
||See [[Protein primary, secondary, tertiary and quaternary structure]].
 +
 +
{Common secondary structures are energetically favored because
 +
|type="[]"}
 +
+ They optimize main-chain hydrogen bonds.
 +
- They represent all possible conformations.
 +
- They maximize clashes between atoms.
 +
+ They minimize clashes between atoms.
</quiz>
</quiz>

Revision as of 23:15, 23 June 2018

1. How many bonded atoms are required to constitute a dihedral (torsion) angle, such as phi or psi?

None
1
2
3
4
5
→
The phi angle is defined by (1) the carboxy carbon from the previous amino acid; (2) N in the amino acid containing the phi bond; (3) Cα in the amino acid containing the phi bond; and (4) the carboxy carbon of the amino acid containing the phi bond.

2. The number of phi and psi angles in an isolated amino acid (not in a polypeptide chain) is:

None
1
2
3
4
5
→The phi angle involves the carboxy carbon of the previous amino acid in a polypeptide chain. The psi angle involves the N of the subsequent amino acid. Therefore an isolated single amino acid has neither phi nor psi angles.

3. The number of atoms held into a geometric plane by a peptide bond is:

3
4
5
6
7
8
→

Questions below may have more than one correct answer.

4. Phi and psi angles directly determine

Primary structure.
Secondary structure.
Tertiary structure.
Quaternary structure.
→See Protein primary, secondary, tertiary and quaternary structure.

5. Alpha helices are compatible with

All possible phi-psi angle combinations.
A limited range of phi-psi angle combinations.
A limited range of phi angles with all possible psi angles.
A limited range of psi angles with all possible phi angles.
→See Protein primary, secondary, tertiary and quaternary structure.

6. Common secondary structures are energetically favored because

They optimize main-chain hydrogen bonds.
They represent all possible conformations.
They maximize clashes between atoms.
They minimize clashes between atoms.

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