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7 Cards in this Set
- Front
- Back
alpha helix
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3.6 aa per turn
5.4 Å per turn no Gly or Pro psi is 0 to -70 degrees rich in Ala and Leu as they are small and fit into the hydrophobic inside large dipole moment |
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beta sheet
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psi between 90 and 180 degrees
parallel: weaker H bonds (6.5 Å) antiparallel: more direct/stronger H bonds (7 Å) |
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type I turn
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Pro is 2nd aa out of 4
carbonyl of 1st aa hydrogen bonds with nitrogen's hydrogen of the 4th aa 6% of Pro is in cis, most of which are in these beta turns |
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type II turn
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Gly is 3rd aa out of 4
1st aa's carbonyl hydrogen bonds with hydrogen on amine of 4th aa |
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alpha-keratin
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-- 2 right-handed alpha helices wrapped in parallel, forming a left-handed helix overall
-- 5.2Å per turn instead of the alpha helix 5.4Å -- hydrophobic interface -- rich in hydrophobic residues (Ala, Val, Leu, Ile, Met, Phe) -- disulfide bonds increase strength (rhino horn has 18% aa involved in disulfide bonds) |
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Collagen
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phi -51, psi 153
right-handed twist overall of 3 left-handed alpha chains rich in Gly, Ala, Pro, 4-Hyp Gly-X-Y X often Pro Y often 4-Hyp |
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Silk fibroin (Beta keratin)
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Beta sheets with hydrogen bonding and extensive van der Waals interactions between sheets
doesn't stretch because B conformation is already highly extended, but it is flexible because the van der Waals interactions can scoot over a few amino acids antiparallel beta sheets rich in Ala and Gly (often alternating), help stack the sheets tightly |