Primary sequence contribution to optical function of the eye lens

Mahendiran, K., Elie, C., Nebel, J-C., Ryan, A. and Pierscionek, B.K. (2014) Primary sequence contribution to optical function of the eye lens. Scientific Reports, 4, p. 5195. ISSN (online) 2045-2322

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Abstract

The crystallins have relatively high refractive increments compared to other proteins. The Greek key motif in βγ-crystallins was compared with that in other proteins, using predictive analysis from a protein database, to see whether this may be related to the refractive increment. Crystallins with Greek keys motifs have significantly higher refractive increments and more salt bridges than other proteins with Greek key domains. Specific amino acid substitutions: lysine and glutamic acid residues are replaced by arginine and aspartic acid, respectively as refractive increment increases. These trends are also seen in S-crystallins suggesting that the primary sequence of crystallins may be specifically enriched with amino acids with appropriate values of refractive increment to meet optical requirements. Comparison of crystallins from five species: two aquatic and three terrestrial shows that the lysine/arginine correlation with refractive increment occurs in all species investigated. This may be linked with formation and maintenance of salt bridges.

Item Type: Article
Research Area: Allied health professions and studies
Biological sciences
Faculty, School or Research Centre: Faculty of Science, Engineering and Computing
Faculty of Science, Engineering and Computing > School of Computing and Information Systems
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Depositing User: Davina Omar
Date Deposited: 23 Apr 2014 11:18
Last Modified: 05 Mar 2015 15:41
URI: http://eprints.kingston.ac.uk/id/eprint/28270

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