Biochemistry 2280A Study Guide - Midterm Guide: Fibroin, Alpha Helix, Coiled Coil

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Biochemistry 2280 Midterm
Protein Structure
Understand peptides
- small number of joined residues
- polypeptides are many of them
- one end of peptide has a free amino group (N-terminal)
- the other has a free carboxyl group (C-terminal)
- additional amino acids are added to the C terminal; peptides are written N-terminal first
- 5 N-C-C-N-C-C-N-C-C 3
- side chains project from this backbone off of the carbons
Distinguish between primary and secondary protein structure
primary
simply the sequence of residues making up the protein
involves only the covalent bonds linking residues together
the minimum size is about 50 residues; smaller than this are just peptides
the largest protein so far discovered has 30,000 residues
average molecular weight of a residue is about 110 Da
secondary
local folding pattern of the backbone
stabilized by hydrogen bonds
- between backbone N-H and C=O groups
most common forms are alpha helix and beta sheets
- also some like loops, helices, and irregular conformations
silk fibroin consists of mostly beta sheets
keratin has lots of alpha structures (makes up hair)
most proteins have both alpha and beta structures; plus other less
regular structure
primary sequence determines the type of structure formed
Describe the characteristics of an alpha helix and beta sheet
alpha helix
coil string arrangement
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