Solution conformation of a tetradecapeptide stabilized by two di-n-propyl glycine residues

Sarojini, Vijayalekshmi and Rao, Balaji R and Ragothama, S and Balaram, Padmanabhan (2010) Solution conformation of a tetradecapeptide stabilized by two di-n-propyl glycine residues. In: Journal of Peptide Science, 16 (8). pp. 430-436.

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Abstract

The solution conformation of a designed tetradecapeptide Boc-Val-Ala-Leu-Dpg-Val-Ala-Leu-Val-Ala-Leu-Dpg-Val-Ala-Leu-OMe (Dpg-14) containing two di-n-propyl glycine (Dpg) residues has been investigated by H-1 NMR and circular dichroism in organic solvents. The peptide aggregates formed at a concentration of 3 mm in the apolar solvent CDCl3 were broken by the addition of 12% v/v of the more polar solvent DMSO-d(6). Successive NiH <-> Ni+1H NOEs observed over the entire length of the sequence in this solvent mixture together with the observation of several characteristic medium-range NOEs support a major population of continuous helical conformations for Dpg-14. Majority of the observed coupling constants ((3)(alpha)(JNHC)(H)) also support phi values in the helical conformation. Circular dichroism spectra recorded in methanol and propan-2-ol give further support in favor of helical conformation for Dpg-14 and the stability of the helix at higher temperature. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.

Item Type:	Journal Article
Publication:	Journal of Peptide Science
Publisher:	John Wiley and Sons
Additional Information:	Copyright of this article belongs to John Wiley and Sons.
Keywords:	di-n-propyl glycine;nuclear Overhauser effect;helical conformation;tetradecapeptide
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre)
Date Deposited:	24 Aug 2010 06:39
Last Modified:	19 Sep 2010 06:14
URI:	http://eprints.iisc.ac.in/id/eprint/31326

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