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

Authors
Type
Published Article
Journal
The Journal of Physical Chemistry B
1520-5207
Publisher
American Chemical Society
Publication Date
Volume
117
Issue
49
Pages
15436–15443
Identifiers
DOI: 10.1021/jp405159v
PMID: 23972032
Source
Medline
License
Unknown

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 related to the fact that the C-terminal domain is more structurally stable than the N-terminal domain. We correlate the vibrational couplings to known energy dissipation mechanisms and reveal their origin.

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