Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles.

ABSTRACT: The eye lens is packed with soluble crystallin proteins, providing a lifetime of transparency and light refraction. gamma-Crystallins are major components of the dense, high refractive index central regions of the lens and generally have high solubility, high stability and high levels of cysteine residues. Human gammaC belongs to a group of gamma-crystallins with a pair of cysteine residues at positions 78 and 79. Unlike other gamma-crystallins it has relatively low solubility, whereas mouse gammaC, which has the exposed C79 replaced with arginine, and a novel mouse splice variant, gammaCins, are both highly soluble. Furthermore, human gammaC is extremely stable, while the mouse orthologs are less stable. Evolutionary pressure may have favoured stability over solubility for human gammaC an

SUBMITTER: Purkiss AG 

PROVIDER: S-EPMC2034304 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature