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Effects of alternative side chain pairings and reverse turn sequences on antiparallel sheet structure in beta-peptide
Joseph M Langenhan1, Samuel H Gellman
1Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, Wisconsin 53706, USA.
Abstract:
[structure: see text] We describe a series of beta-peptide hexamers that allow us to explore relationships between sequence and hairpin folding. Different reverse turn segments are compared at the central two positions, and the outer residues allow a variety of interstrand side chain-side chain pairings. NMR analysis in methanol demonstrates that several reverse turn and side chain pairing arrangements are compatible with antiparallel beta-peptide sheet structure; however, none of the beta-peptides folds in water.
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