4.5 Article

Temperature dependence of the internal dynamics of a protein in an aqueous solvent: Decoupling from the solvent viscosity

期刊

CHEMICAL PHYSICS
卷 424, 期 -, 页码 12-19

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.chemphys.2013.02.026

关键词

Protein; Water; Solution; Dynamics; Neutron scattering

资金

  1. Scientific User Facilities Division, Office of Basic Energy Sciences, US Department of Energy (DOE)
  2. Office of Biological and Environmental Research, US DOE [ERKP291]
  3. US DOE [DE-AC05-00OR22725]

向作者/读者索取更多资源

We have recently observed decoupling of the dynamics of a protein from its aqueous solvent [Chu et al., JPCL 3 (2012) 380]; here we report the more detailed studies. We analyzed quasielastic neutron scattering data from a 40 mg/ml solution of lysozyme in (D2O)(8)(LiCl) and (H2O)(8)(LiCl). The internal dynamics of lysozyme exhibited super-Arrhenius temperature dependence with no crossover to a different regime down to at least 200 K. The decoupling of the internal protein dynamics from the viscosity of its aqueous solvent is evident. The temperature dependence of the protein dynamics indicates an apparent dynamic arrest at a temperature above 190 K, whereas the glass transition temperature for the solvent is around 135-140 K. The internal dynamics of the solvated protein is coupled to the dynamics of its hydration shell, not of the bulk solvent, which is qualitatively altered by the salt to defer the dynamic arrest to 135-140 K. (C) 2013 Elsevier B. V. All rights reserved.

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