Chapter 5 Flashcards
Primary structure
Sequence of amino acids in a polypeptide chain
Alpha helix
- complete turn has about 3.6 residues
- stability from hydrogen bonds
- proline can only be accommodated by the first turn
Beta sheet
Zig zag or pleated pattern
-parallel or antiparallel
Antiparallel beta sheet
Hydrogen bonds run parallel to polypeptide backbone
Beta turn
Involved 4 aminoacyl residues
Loops
Contain more than 4 aminoacyl residues
Monomeric
One polypeptide chain
Dimeric
2 polypeptide chains
Homodimers
Two copies of the same polypeptide chain
Heterodimers
The 2 chains differ
Chaperones
Prevent aggregation
hsp70 binds short sequences of hydrophobic amino acids that emerge while a new polypeptide is forming
Aggregates
Complexes of partly unfolded polypeptides
Collagen
- glycine, hydroxyproline, and hydroxylysine
- triple helix has 3.3 residues per turn
Globular proteins
Compact, roughly spherical molecules