Abstract
We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.
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Acknowledgements
The authors thank Melanie Cocco and AJ Shaka for helpful discussions and Evgeny Fadeev for excellent NMR facility management. This work was supported by NSF-CAREER CHE-0847375 and NIH RO1GM-78528.
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Brubaker, W.D., Martin, R.W. 1H, 13C, and 15N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V. Biomol NMR Assign 6, 63–67 (2012). https://doi.org/10.1007/s12104-011-9326-1
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DOI: https://doi.org/10.1007/s12104-011-9326-1