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

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.