tertiary structure 9/28 Flashcards
1
Q
what is a protein’s 3D structure (tertiary and quaternary) determined by
A
amino acid sequence
2
Q
what can help determine 3D structures
A
-x ray diffraction and NMR spectroscopy
3
Q
what is x ray diffraction
A
protein crystal held in beam of x rays and x ray photons deflect and pattern of dots used to calculate protein that caused diffraction (need substaintale size crystal to start)
4
Q
what is NMR spectroscopy
A
- measure of spin of protons
- shows range of motions molecules go through
5
Q
fibrous proteins have predominantly what type of structure
A
secondary
6
Q
alpha keratin
A
- intermediate filament family of cytoskeletal proteins
- primary structure (Z-X-X-Z-X-X-X)n where X is usually cysteine (cross linking sidechain), and Z is a hydrophobic residue
- alpha helical conformation since on turn of helix is 3.6 residues helix will have a hydrophobic stripe
- 2 right handed helices twist together left handed to form coiled coil, held tightly together by hydrophobic stripes
- in each coiled coil one of polypeptides is type I (acidic) and other is type II (basic)
- coiled coils associate together with others to make larger structures such as protofilaments, protofibrils, intermediate filaments, hair cells, hair
7
Q
collagen
A
- major structural filament in animal connective tissue
- primary structure: gly-X-pro or gly-X-hydroxyproline where x is any amino acid residue
- gly and pro form left handed helix with pitch 9.4 A
- three of extended helices form right handed coiled coil
- all gly residues have side chains in spae between three helices
- only gly side chains small enough to fit into position
- mutation substituting anything but gly in this position causes severe birth defects and scury is also caused by lack of collagen
- vitamin C –> hydroxyproline –> collagen
- coiled coils cross linked together by covalent bonds involving lys and hydroxylysine residues
8
Q
fibroin
A
- main component of silk and spider webs
- primary structure consists of repeating pattern (gly-ala)n where ser can be substituted for ala
- each polypeptide chain forms strand of beta sheet with gly side chains facing one way and ala (ser) chains facing the other
- beta sheets stack with like side chains of adjacent sheets zipping together forming very strong, non elastic fiber
- various types of silk have varying amounts of a random coil configuration included within a strand and the more of this random coil the more elastic the fibers