A short linear peptide that folds into a native stable β-hairpin in aqueous solution

Abstract

The conformational properties of a 16 residue peptide, corresponding to the second β-hairpin of the B1 domain of protein G, have been studied by nuclear magnetic resonance spectroscopy (NMR). This fragment is monomeric under our experimental conditions and in pure water adopts a population containing up to 40% native-like β-hairpin structure. The detection by NMR of a native-like β-hairpin in aqueous solution, reported here for the first time, indicates that these structural elements may have an important role in the early steps of protein folding. It also provides a good model to study in detail the sequence determinants of β-hairpin structure stability, as has been done with α-helices.