Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.

ABSTRACT: The eye lens crystallins represent an ideal target for studying the effects of aging on protein structure. Herein we examine separately the water-soluble (WS) and water-insoluble (WI) crystallin fractions and identify sites of isomerization and epimerization. Both collision-induced dissociation and radical-directed dissociation are needed for detection of these non-mass-shifting post-translational modifications. Isomerization levels differ significantly between the WS and the WI fractions from sheep, pig, and cow eye lenses. Residues that are most susceptible to isomerization are identified site-specifically and are found to reside in structurally disordered regions. However, isomerization in structured domains, although less common, often yields more dramatic effects on solubility. Numero

SUBMITTER: Lyon YA 

PROVIDER: S-EPMC5387677 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature