Circular dichroism of designed peptide helices and β-hairpins: analysis of trp- and tyr-rich peptides

Mahalakshmi, Radhakrishnan ; Shanmugam, Ganesh ; Polavarapu, Prasad L. ; Balaram, Padmanabhan (2005) Circular dichroism of designed peptide helices and β-hairpins: analysis of trp- and tyr-rich peptides ChemBioChem, 6 (12). pp. 2152-2158. ISSN 1439-4227

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Official URL: http://www3.interscience.wiley.com/journal/1121382...

Related URL: http://dx.doi.org/10.1002/cbic.200500152

Abstract

VCD versus ECD spectroscopy. Peptides rich in aromatic residues yield anomalous far-UV electronic circular dichroism (ECD) spectra that preclude secondary structure assignment. The utility of vibrational circular dichroism (VCD) in conformation analysis is demonstrated by using a set of well-defined peptide helices and hairpins containing proximal aromatic residues.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons, Inc.
Keywords:Aromatic Compounds; Circular Dichroism; Hairpin Peptides; Helical Structures; Peptides
ID Code:4616
Deposited On:18 Oct 2010 07:20
Last Modified:16 May 2016 15:14

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