lecture 18 - protein structure: beta sheets Flashcards
1
Q
explain beta-sheet structure
A
- repetitive phi/psi angles
- zig-zag comfirmations of backbone
- not formed by a contiguous region of amino acid sequence
- minimum of 2 beta strands come together to form a beta sheet
2
Q
what is a beta sheet stabilized by?
A
H-bonds between strands (can be parallel or anti-parallel)
3
Q
explain anti-parallel H-bonds between beta sheets
A
- R groups on adjacent strands are oriented in the same direction (e.g. all R groups are above the plane)
- H-bonds are perpendicular to strands and in the plane of the sheet
4
Q
explain parallel H-bonds between beta sheets
A
-some R groups are above the plane, some R groups are below the plane
5
Q
explain the relationship between parallel H bonds and an amphipathic B-sheet
A
- can create an amphipathic B-sheet by having hydrophobic R groups on face and hydrophilic groups on another face
- implies mechanism for folding B-sheets to bury hydrophobic face
6
Q
beta sheets often have a twist (not strictly planar), what does this mean? what does this require?
A
- have a mix of anti-parallel and parallel H-bonds
- need more than 2 strands
7
Q
explain how secondary structures link together
A
- flexible regions (have primary structure) allow the secondary structure to fold into 3D fold
- have alternate folding pattern: parallel beta sheet with alpha helix on top, etc.
8
Q
define motif
A
collection of secondary structural elements