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Role of Nonplanar Peptide Unit in Regular Polypeptide Helices - New Model for Pply-Beta-Benzyl-L-Aspartate

Nambudripad, R and Bansal, M and Sasisekharan, V (1981) Role of Nonplanar Peptide Unit in Regular Polypeptide Helices - New Model for Pply-Beta-Benzyl-L-Aspartate. In: International Journal of Peptide & Protein Research, 18 (4). pp. 374-382.

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Abstract

The effect of non-planarity of the peptide unit on helical structures stabilized by intrachain hydrogen bonds is discussed. While the present calculations generally agree with those already reported in the literature for right-handed helical structures, it is found that the most stable left-handed structure is a novel helix, called the delta-helix. Its helical parameters are close to these reported for poly-beta-benzyl-L -aspartate. Conformational energy calculations show that poly-beta-benzyl-L -aspartate with the delta-helical structure is considerably more stable than the structure it is generally believed to take up (the omega-helix) by about 15 kcal/mol-residue.

Item Type: Journal Article
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 17 Feb 2012 06:13
Last Modified: 17 Feb 2012 06:13
URI: http://eprints.iisc.ernet.in/id/eprint/43262

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