Mahendiran, K., Elie, Céline, Nebel, Jean-Christophe, Ryan, Ali and Pierscionek, Barbara K. (2014) Primary sequence contribution to the optical function of the eye lens. Scientific Reports, 4 (1). p. 5195. ISSN 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: | Journal Article |
|---|---|
| Keywords: | Protein function predictions, Proteins |
| Faculty: | ARCHIVED Faculty of Health, Social Care & Education (until September 2018) |
| Depositing User: | Lisa Blanshard |
| Date Deposited: | 18 Feb 2021 16:03 |
| Last Modified: | 09 Sep 2021 19:01 |
| URI: | https://arro.anglia.ac.uk/id/eprint/706301 |
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