Use of essential and molecular dynamics to study gamma B-crystallin unfolding after non-enzymic post-translational modificationsCrabbe, 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 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/s1476-9271(03)00048-3 Abstract/SummaryEssential 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.
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