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Use of essential and molecular dynamics to study gamma B-crystallin unfolding after non-enzymic post-translational modifications

Crabbe, M. J. C., Cooper, L. R. and Corne, D. W. (2003) Use of essential and molecular dynamics to study gamma B-crystallin unfolding after non-enzymic post-translational modifications. Computational Biology and Chemistry, 27 (4-5). pp. 507-510. ISSN 1476-9271

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To link to this item DOI: 10.1016/s1476-9271(03)00048-3

Abstract/Summary

Essential and Molecular Dynamics (ED/MD) have been used to model the conformational changes of a protein implicated in a conformational disease-cataract, the largest cause of blindness in the world-after non-enzymic post-translational modification. Cyanate modification did not significantly alter flexibility, while the Schiff's base adduct produced a more flexible N-terminal domain, and intra-secondary structure regions, than either the cyanate adduct or the native structure. Glycation also increased linker flexibility and disrupted the charge network. A number of post-translational adducts showed structural disruption around Cys15 and increased linker flexibility; this may be important in subsequent protein aggregation. Our modelling results are in accord with experimental evidence, and show that ED/MD is a useful tool in modelling conformational changes in proteins implicated in disease processes. (C) 2003 Published by Elsevier Ltd.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10710
Uncontrolled Keywords:cataract, crystallins, lens, supercomputer, II-CRYSTALLIN, PROTEIN, SIMULATIONS

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