Abstract
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 40mg/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 200K. 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 190K, whereas the glass transition temperature for the solvent is around 135–140K. 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 135–140K.
Published Version
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