tertiary structure 9/28 Flashcards

1
Q

what is a protein’s 3D structure (tertiary and quaternary) determined by

A

amino acid sequence

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2
Q

what can help determine 3D structures

A

-x ray diffraction and NMR spectroscopy

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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)

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4
Q

what is NMR spectroscopy

A
  • measure of spin of protons
  • shows range of motions molecules go through
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5
Q

fibrous proteins have predominantly what type of structure

A

secondary

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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
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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
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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
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