Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.

ABSTRACT: Cataracts is a misfolding protein disease in which one of the major components is the γD-crystallin protein. The conformational structure of the aggregated γD-crystallin and the interactions that cause aggregation are largely unknown. A recent experimental two-dimensional infrared (2DIR) spectroscopy study determined that the C-terminal domain has a high propensity to form β-sheets whereas the N-terminal domain forms a disordered structure in the fiber state. We present a combined computational molecular dynamics and infrared spectroscopy study of the local dynamics of these domains. The computed 2DIR signals agree remarkably well with experiment. We show that the two domains, both of which have a Greek key structural fold, experience different electrostatic environments, which may be rela

SUBMITTER: Lam AR 

PROVIDER: S-EPMC3865159 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature