Chapter 4 Flashcards

1
Q

5 constraints on alpha helix stability

A
  • electrostatic repulsion between residues
  • the bulkiness of adjascent R groups
  • the interactions of residues spaced by 3-4 residues
  • the occurence of proline and glycine
  • the interaction of amino acids at each end of the helix
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2
Q

parallel beta sheets vs anti parallel beta sheets

A
  • strands run in the same N to C direction

- strands run in opposite

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3
Q

what determines tertiary structure

A

amino acid sequence

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4
Q

quaternary structure is what by what

A

subunits held together by non covalent interactions

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5
Q

3 fibrous proteins and 2 globular proteins

A
  • keratin, collagen, silk

- myoglobin, hemoglobin

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6
Q

examples and primary structure of keratin

A
  • hair, nails, horns

- contains a seven repeat pattern where positions a and d are hydrophobic

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7
Q

the coiled coil of keratin is

A

two right handed helicies around each other in a left handed fashion

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8
Q

the individual units of keratin are

A

linked together through disulfide bonds

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9
Q

collage examples and primary structure

A
  • tendons and skin

- repeats of Gly-Pro-hydroxyprol

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10
Q

the coiled coil of collagen is

A

three left handed helicies around each other in a right handed fashion

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