Effects of alternative side chain pairings and reverse turn sequences on antiparallel sheet structure in beta-peptide hairpins |
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Authors: | Langenhan Joseph M Gellman Samuel H |
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Institution: | Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, Wisconsin 53706, USA. |
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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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