Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface.

ABSTRACT: In the lens of the eye the ordered arrangement of the major proteins, the crystallins, contributes to lens transparency. Members of the beta/gamma-crystallin family share common beta-sheet rich domains and hydrophobic regions at the monomer-monomer or domain-domain interfaces. Disruption of these interfaces, due to post-translational modifications, such as deamidation, decreases the stability of the crystallins. Previous experiments have failed to define the structural changes associated with this decreased stability. Using hydrogen/deuterium exchange with mass spectrometry (HDMS), deamidation-induced local structural changes in betaB2-crystallin were identified. Deamidation was mimicked by replacing glutamines with glutamic acids at homologous residues 70 and 162 in the monomer-monomer in

SUBMITTER: Takata T 

PROVIDER: S-EPMC2926248 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature