β-hairpin and β-sheet formation in designed linear peptides

Marina Ramírez-Alvarado; Tanja Kortemme; Francisco J. Blanco; Luis Serrano

doi:10.1016/S0968-0896(98)00215-6

β-hairpin and β-sheet formation in designed linear peptides

Marina Ramírez-Alvarado, Tanja Kortemme, Francisco J. Blanco, Luis Serrano

Biochemistry and Molecular Biology

Research output: Contribution to journal › Article

116 Scopus citations

Abstract

Recent knowledge about the determinants of β-sheet formation and stability has notably been improved by the structural analysis of model peptides with β-hairpin structure in aqueous solution. Several experimental studies have shown that the turn region residues can not only determine the stability, but also the conformation of the β-hairpin. Specific interstrand side-chain interactions, hydrophobic and polar, have been found to be important stabilizing interactions. The knowledge acquired in the recent years from peptide systems, together with the information gathered from mutants in proteins, and the analysis of known protein structures, has led to successful design of a folded three-stranded monomeric β-sheet structure. Copyright (C) 1999 Elsevier Science Ltd.

Original language	English (US)
Pages (from-to)	93-103
Number of pages	11
Journal	Bioorganic and Medicinal Chemistry
Volume	7
Issue number	1
DOIs	https://doi.org/10.1016/S0968-0896(98)00215-6
State	Published - Jan 1 1999

Keywords

NMR
Peptides
Protein folding
β-hairpin
β-sheet

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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Ramírez-Alvarado, M., Kortemme, T., Blanco, F. J., & Serrano, L. (1999). β-hairpin and β-sheet formation in designed linear peptides. Bioorganic and Medicinal Chemistry, 7(1), 93-103. https://doi.org/10.1016/S0968-0896(98)00215-6

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