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

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

Research output: Contribution to journalArticle

116 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)93-103
Number of pages11
JournalBioorganic and Medicinal Chemistry
Volume7
Issue number1
DOIs
StatePublished - Jan 1999
Externally publishedYes

Fingerprint

Peptides
Structural Models
Mutant Proteins
Hydrophobic and Hydrophilic Interactions
Structural analysis
Conformations
Proteins

Keywords

  • β-hairpin
  • β-sheet
  • NMR
  • Peptides
  • Protein folding

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

β-hairpin and β-sheet formation in designed linear peptides. / Ramirez-Alvarado, Marina; Kortemme, Tanja; Blanco, Francisco J.; Serrano, Luis.

In: Bioorganic and Medicinal Chemistry, Vol. 7, No. 1, 01.1999, p. 93-103.

Research output: Contribution to journalArticle

Ramirez-Alvarado, Marina ; Kortemme, Tanja ; Blanco, Francisco J. ; Serrano, Luis. / β-hairpin and β-sheet formation in designed linear peptides. In: Bioorganic and Medicinal Chemistry. 1999 ; Vol. 7, No. 1. pp. 93-103.
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