Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,...Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,computational study,and X-ray structures.The turn loop of thisβ-hairpin motif accommodates different two-residueα-amino acid sequences from the highly flexible Gly-Gly,to the more restricted D-Pro-Gly.The presence ofα-amino acid side chains enhances the stabilities of theβ-hairpins with the exception of D-Pro-Gly-which results in destabilization.Based on this hairpin/turn motif,a variety of different dipeptide sequences ofα-amino acids which rarely occur inβ-turns can be introduced and presented as two-residue loops.展开更多
基金supported by the National Natural Science Foundation of China(No.21778012 to Z.L.Lu,21801020 to R.Liu)the American Chemical Society–Petroleum Research Fund(PRF#58364-ND7,to B.Gong)+1 种基金the Center for Computational Research(CCR)(to D.P.Miller and E.Zurek)Hofstra University(to D.P.Miller)。
文摘Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,computational study,and X-ray structures.The turn loop of thisβ-hairpin motif accommodates different two-residueα-amino acid sequences from the highly flexible Gly-Gly,to the more restricted D-Pro-Gly.The presence ofα-amino acid side chains enhances the stabilities of theβ-hairpins with the exception of D-Pro-Gly-which results in destabilization.Based on this hairpin/turn motif,a variety of different dipeptide sequences ofα-amino acids which rarely occur inβ-turns can be introduced and presented as two-residue loops.
