Role of non-planar peptide unit in regular polypeptide helices: a new model for poly-beta-benzyl-L-aspartate

Namboodripad, R. ; Bansal, M. ; Sasisekharan, V. (1981) Role of non-planar peptide unit in regular polypeptide helices: a new model for poly-beta-benzyl-L-aspartate International Journal of Peptide & Protein Research, 18 (4). pp. 374-382. ISSN 0367-8377

Full text not available from this repository.

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:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
ID Code:79560
Deposited On:27 Jan 2012 13:05
Last Modified:01 Jul 2012 06:34

Repository Staff Only: item control page