Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.

ABSTRACT: Aberrant protein interactions can lead to aggregation and insolubilization, such as occurs during cataract formation. Deamidation, a prevalent age-related modification in the lens of the eye, decreases stability of the major lens proteins, crystallins. The mechanism of deamidation altering interactions between αA-crystallin and βB2-crystallin was investigated by detecting changes in solvent accessibility upon complex formation during heating. Solvent accessibility was determined by measuring hydrogen/deuterium exchange levels of backbone amides by high-resolution mass spectrometry. Deuterium levels in wild type βB2-crystallin increased 50-60% in both domains following complex formation with αA-crystallin. This increased solvent accessibility indicated a general loosening along the backbone

SUBMITTER: Lampi KJ 

PROVIDER: S-EPMC3490024 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature