期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 12, 页码 4246-4249出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja2002346
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资金
- University of Pittsburgh
The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the a-helix, mimicry of protein beta-sheets is less understood. We report here the aqueous folding behavior of a prototype alpha-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different beta-amino acid monomers. Our results provide a folding propensity scale for beta-residues in a protein beta-sheet context as well as high-resolution structures of several mixed-backbone alpha/beta-peptide hairpins in water.
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