Study of the γd-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: Experiment and simulation
| Autor: | Sean D. Moran, Nicholas K. Preketes, Shaul Mukamel, Tianqi O. Zhang, Martin T. Zanni, A. R. Lam |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Protein Structure
Secondary Spectrophotometry Infrared Infrared Infrared spectroscopy Molecular Dynamics Simulation Protein Structure Secondary Article Molecular dynamics Protein structure Engineering Crystallin Spectrophotometry Materials Chemistry medicine Physical and Theoretical Chemistry Spectroscopy medicine.diagnostic_test Chemistry Dissipation Crystallins Protein Structure Tertiary Surfaces Coatings and Films Crystallography Chemical physics Chemical Sciences Physical Sciences Tertiary |
| Zdroj: | Lam, AR; Moran, SD; Preketes, NK; Zhang, TO; Zanni, MT; & Mukamel, S. (2013). Study of the γd-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: Experiment and simulation. Journal of Physical Chemistry B, 117(49), 15436-15443. doi: 10.1021/jp405159v. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/81n7f4sq The journal of physical chemistry. B, vol 117, iss 49 |
| DOI: | 10.1021/jp405159v. |
| Popis: | 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. © 2013 American Chemical Society. |
| Databáze: | OpenAIRE |
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