De novo design: backbone conformational constraints in nucleating helices and beta-hairpins

Balaram, P (1999) De novo design: backbone conformational constraints in nucleating helices and beta-hairpins. In: Journal of Peptide Research, 54 (3). pp. 195-199.

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Abstract

A modular approach to synthetic protein design is being developed using conformationally constrained amino acid as stereochemical directors of polypeptide chain folding. An overview of studies aimed at constructing peptide helices using alpha,alpha-dialkyated residues and beta-hairpins using D-Pro as a turn nucleator is presented. The construction of helix-helix motifs and three- and four-stranded structures has been achieved using non-protein amino acids to stabilize specific elements of secondary structures.

Item Type:	Journal Article
Publication:	Journal of Peptide Research
Publisher:	John Wiley and Sons
Additional Information:	Copyright for this article belongs to John Wiley and Sons.
Keywords:	De novo design;Helices;beta-hairpins;Peptide design
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	30 Sep 2004
Last Modified:	13 Jan 2012 07:59
URI:	http://eprints.iisc.ac.in/id/eprint/2072

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