title: Stereospecific peptide folds. A rationally designed molecular bracelet.
abstract: A canonical planar beta-hairpin peptide, stereochemically reengineered into a semicircular bracelet type motif by L-to-D stereochemical inversion in two pairs of its cross-strand neighbor residues, displays protein like ordering including two-state behavior in H2O, which is unusual for a small peptide of this size.
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Bombay, Numbai-400076, India.
authors.forename: Soumendra
authors.initials: S
authors.lastname: Rana
authors.forename: Bijoy
authors.initials: B
authors.lastname: Kundu
authors.forename: Susheel
authors.initials: S
authors.lastname: Durani
mesh_terms: D004121:Dimethyl Sulfoxide / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013237:Stereoisomerism; D014867:Water / Q000737:chemistry
chemical_list: D010455:Peptides; D014867:Water; D004121:Dimethyl Sulfoxide