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Curr Opin Chem Biol. 1998 Dec;2(6):717-25.

Minimal model systems for beta sheet secondary structure in proteins.

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  • 1Department of Chemistry University of Wisconsin Madison WI 53706 USA. gellman@chem.wisc.edu

Abstract

Use of model systems to explore the forces that control beta sheet formation was stymied for many years by the perception that small increments of beta sheet necessarily aggregate. Recently, however, a number of short peptides (9-16 residues in length) that fold into two-stranded antiparallel beta sheets ('beta hairpins') have been reported; several short peptides (20-24 residues in length) that fold into three-stranded antiparallel beta sheets have also been described. These model systems are beginning to provide fundamental insights into the origins of beta sheet conformational stability.

PMID:
9914187
[PubMed - indexed for MEDLINE]
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