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BCH40332ndrystructure

BCH40332ndrystructure - 1429/5 Protein examples of 2°...

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Unformatted text preview: 1429/5 Protein examples of 2° structure—fibrous proteins (insoluble in water due to high hydrophobic amino acid content) OL- -keratin—(hair, nails, fur) 4, Vex/V3141 composed of right- handed OL- helix pept1de chains (3 6 residues/tum) coiled coilwlike rope strands, each strand 1s a right- -handed Ot- -helix (the coiling forms a left-handed helix even though each strand is right-handed) L [#45411 the coiling makes the protein stronger red/«4 Li a lot of hydrophobic residues packed together where the strands M::J’T touch. ignisw “ R, disulfide bonds form between the strands (ex: hair styling, f ’) (H , \t M permanents) Rhinoceros horn 18% of amino acids in disulfide . “ ifle—v bonds, highly cross- -linked. "A“ Hm» f I'M-9): ”~ “Mime collagen—(skin, bone marrow, cartilage, tendon) / 3 1W1”! ‘5 chm} composed of left-handed oc-helix peptide chains, triple helix (3.0 residues/turn) coiled coil—like rope strands, each strand is a left—handed oc—helix (the coiling forms a right-handed helix even though each strand is left-handed) Gly-X-Pro or Gly-X-HyPro repeated sequences in peptide chain High Pro content allows tight turns, so therefore only 3.0 residues/tum Triple helix stronger tensile strength than steel of same diameter. Proline —> HydroxkyProlineO carried out by prolyl hydroxylase (ascorbic acid dependent) 1e. -« (1. ~ l NH” cx'iew ——-) NW“ CM" 0")” 1V! kw Scurvy: weakend collagen due to vitamin C (ascorbic acid) deficiency a + scorblitus (Greek or Latin for scurvy) not scurvy, like a + moral = not moral COW" “1"“) symptoms— — joint pain, bruising, teeth loosen, skin lesions, weak tendons, blood vessels rupture Silk—Fibroin protein, B-sheets, a lot of Ala, Gly residues so close packing of R groups possible Silk doesn’t stretch much, highly extended but very flexible due to hydrophobic association of R groups ...
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