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Circular Dichroism of Designed Peptide Helices and \beta -Hairpins: Analysis of Trp-and Tyr-Rich Peptides

Mahalakshmi, Radhakrishnan and Shanmugam, Ganesh and Polavarapu, Prasad L and Balaram, Padmanabhan (2005) Circular Dichroism of Designed Peptide Helices and \beta -Hairpins: Analysis of Trp-and Tyr-Rich Peptides. In: ChemBioChem, 6 (12). pp. 2152-2158.

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Abstract

Carefullychosen peptide systems can provide valuable insights into the details of protein folding. Construction of the secondarystructures most commonlyobserved in proteins, namely a-helices and b-sheets, from constrained amino acid residues allows detailed investigation of the factors driving the folding and stabilityof these structural scaffolds.

Item Type: Journal Article
Additional Information: The copyright belongs to WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Keywords: aromatic compounds;circular dichroism;hairpin peptides;helical structures;peptides
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 29 Dec 2005
Last Modified: 19 Sep 2010 04:22
URI: http://eprints.iisc.ernet.in/id/eprint/4712

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