Stereospecific peptide folds. A rationally designed molecular bracelet.
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.
Rana
Soumendra
S
Department of Chemistry, Indian Institute of Technology, Bombay, Numbai-400076, India.
Kundu
Bijoy
B
Durani
Susheel
S
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
D010455:Peptides; D014867:Water; D004121:Dimethyl Sulfoxide