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Achary, M.S. and Nagarajaram, H.A. (2009) Effects of Disease Causing Mutations on the Essential Motions in Proteins. Journal of Biomolecular Structure and Dynamics, 26 (5). pp. 609-623. ISSN 0739-1102

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Abstract

This study embodies a detailed comparative analysis of the essential motions of the Wild type and the eight different disease mutant forms of the Human CYP1b1. The mutations considered in this study have been implicated in Primary Congenital Glaucoma, an in-born, genetic disorder associated with eye-abnormality. The principal component analysis for Wild type and the Mutants was carried out using the stabilized molecular dynamics trajectories, which ranged from 35 to 45 nanoseconds. Investigations revealed the nature of the collective motions that characterize functionally relevant 'essential motions'. The essential motions in Wild type are characterized by the collective motions of the Substrate Access Channel including the beta-rich domain and the loops in the region of p450-reductase interaction. Comparative analysis of the essential motions of the Wild type and Mutants, especially those involving the functionally important regions indicated distinct differences in their magnitudes as well as the residue-wise distribution. The Mutants in general are associated with higher root mean square fluctuations, and involve some of the relatively intact core regions of the protein, in large collective motions. This study sheds light on the possible effects of disease causing mutations on the large functionally important collective motions in proteins

Item Type: Article
Depositing User: Users 2 not found.
Date Deposited: 26 Aug 2015 11:10
Last Modified: 01 Dec 2017 09:43
URI: http://cdfd.sciencecentral.in/id/eprint/391

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