A short linear peptide that folds into a native stable beta-hairpin in aqueous solution.
The conformational properties of a 16 residue peptide, corresponding to the second beta-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 beta-hairpin structure. The detection by NMR of a native-like beta-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 beta-hairpin structure stability, as has been done with alpha-helices.
Blanco
F J
FJ
European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Rivas
G
G
Serrano
L
L
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D012996:Solutions; D013056:Spectrophotometry, Ultraviolet; D014867:Water
D012996:Solutions; D014867:Water