期刊
EXPERIMENTAL EYE RESEARCH
卷 79, 期 6, 页码 823-831出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exer.2004.05.009
关键词
alpha A-crystallin; cataract; cysteine; lens; beta B1-crystallin; gamma-crystallins; glutathione; homology models; oxidation; sulfinic acid; solvent accessibility
Molecular models of human gamma-crystallins and the 'alpha-crystallin domain' of human alphaA-crystallin have been built based on available related X-ray crystal structures. The accessibilities of the component cysteine, methionine and tryptophan side chains in the crystallin models have been calculated. The reactivities of these cysteines, which are oxidised in cataract, are assessed based on their known modifications and within the context of their location within the 3D models. (C) 2004 Elsevier Ltd. All rights reserved.
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