Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.

ABSTRACT: γ-crystallins are highly specialized proteins of the vertebrate eye lens where they survive without turnover under high molecular crowding while maintaining transparency. They share a tightly folded structural template but there are striking differences among species. Their amino acid compositions are unusual. Even in mammals, γ-crystallins have high contents of sulfur-containing methionine and cysteine, but this reaches extremes in fish γM-crystallins with up to 15% Met. In addition, fish γM-crystallins do not conserve the paired tryptophan residues found in each domain in mammalian γ-crystallins and in the related β-crystallins. To gain insight into important, evolutionarily conserved properties and functionality of γ-crystallins, zebrafish (Danio rerio) γM2b and γM7 were compared with m

SUBMITTER: Chen Y 

PROVIDER: S-EPMC3892301 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature