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Beta-structure of polypeptides in non-aqueous solutions. I. Spectral characteristics of the polypeptide backbone

Raghavendra, K and Ananthanarayanan, VS (1981) Beta-structure of polypeptides in non-aqueous solutions. I. Spectral characteristics of the polypeptide backbone. In: International Journal of Peptide & Protein Research, 17 (4). pp. 412-419.

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Abstract

The optical rotatory features of the beta-structure of the polypeptides in non-aqueous solutions and films cast from these solutions have been investigated. The beta-structure of poly-S-benzyl-L-cysteine, poly-S-carbobenzoxy-L-cysteine and poly-S-benzyl-L-cysteine, poly-S-carbobenzoxy-L-cysteine and poly-O-carbo-bands of their films. The optical rotatory dispersion (ORD) and circular dichroism (CD) spectra of these polypeptides are found to be very similar in both film and solution. In solvents promoting the beta-structure, the polypeptides are characterized by CD troughs in the n-pi* transition region of the peptide chromophore. The ORD spectra are found to be positive in sign throughout the visible and accessible ultraviolet regions and are interpreted in terms of the possible existence of a relatively much larger positive pi-pi* CD bands as compared with the negative n-pi* band. The rotatory data obtained in the non-aqueous solution are compared with those obtained for other poly peptides in aqueous solutions, with respect to the type and extent of beta-structure present.

Item Type: Journal Article
Publication: International Journal of Peptide & Protein Research
Publisher: Munksgaard Int Publ Ltd
Additional Information: Copyright of this article belongs to Munksgaard Int Publ Ltd.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 09 Nov 2011 05:24
Last Modified: 09 Nov 2011 05:24
URI: http://eprints.iisc.ac.in/id/eprint/40754

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