Issue 21, 2004

Stereospecific peptide folds. A rationally designed molecular bracelet

Abstract

A canonical planar β-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.

Graphical abstract: Stereospecific peptide folds. A rationally designed molecular bracelet

Article information

Article type
Communication
Submitted
13 Jul 2004
Accepted
09 Aug 2004
First published
20 Sep 2004

Chem. Commun., 2004, 2462-2463

Stereospecific peptide folds. A rationally designed molecular bracelet

S. Rana, B. Kundu and S. Durani, Chem. Commun., 2004, 2462 DOI: 10.1039/B410532J

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