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- W2067095008 abstract "Knowledge of the secondary structure of antifreeze peptides (AFPs) and glycopeptides (AFGPs) is crucial to understanding the mechanism by which these molecules inhibit ice crystal growth. A polyproline type II helix is perhaps the most widely accepted conformation for active AFGPs; however, random coil and alpha-helix conformations have also been proposed. In this report we present vibrational spectroscopic evidence that the conformation of AFGPs in solution is not random, not alpha-helical, and not polyproline type II. Comparison of AFGP amide vibrational frequencies with those observed and calculated for beta and gamma-turns in other peptides strongly suggests that AFGPs contain substantial turn structure. Computer-generated molecular models were utilized to compare gamma-turn, beta-turn, and polyproline II structures. The gamma-turn motif is consistent with observed amide frequencies and results in a molecule with planar symmetry with respect to the disaccharides. This intriguing conformation may provide new insight into the unusual properties of AFGPs." @default.
- W2067095008 created "2016-06-24" @default.
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- W2067095008 date "1993-09-01" @default.
- W2067095008 modified "2023-10-12" @default.
- W2067095008 title "Evidence for a gamma-turn motif in antifreeze glycopeptides" @default.
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- W2067095008 doi "https://doi.org/10.1016/s0006-3495(93)81167-6" @default.
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