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.

Preview

PDF page154.pdf Download (258kB)

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
Publication:	ChemBioChem
Publisher:	WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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.ac.in/id/eprint/4712

Actions (login required)

View Item