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• W1985251059 abstract "Proton and 13C magnetic resonance studies are reported on the synthetic polypentapeptide of elastin, HCO-(Val(1)-Pro(2)-Gly(3)-Val(4)-Gly(5))n-Val-OMe, where n ∼- 18. Temperature and solvent dependence of peptide NH chemical shift and solvent dependence of peptide carbonyl chemical shift were used to delineate these moieties preliminary to identification of secondary structure. Based on these studies it is proposed, for the organic solvents of dimethyl sulfoxide, methanol, and low-temperature trifluoroethanol, that dynamic hydrogen bonds form in order of decreasing frequency of occurrence between the Val(1) CO and the Val(4) NH (a β-turn), between the Gly(3) NH and the Gly(5) CO (an 11-atom, hydrogen-bonded ring), and a more limited interaction between the Gly(3) CO and the Gly(5) NH (a γ-turn). Arguments are presented that relate the conformational features proposed above to the coacervate, which is a filamentous state." @default.
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• W1985251059 date "1975-07-01" @default.
• W1985251059 modified "2023-09-27" @default.
• W1985251059 title "Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin" @default.
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• W1985251059 doi "https://doi.org/10.1016/0022-2836(75)90184-9" @default.
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