title: Methyl group dynamics as a probe of the protein dynamical transition.
abstract: Hydrated proteins undergo a dynamical transition around 200 K from glasslike to liquidlike motion. Molecular dynamics simulations have been used to study the temperature dependence of the dynamics of ribonuclease A in the hydrated crystal, a model dehydrated powder, and aqueous solution. Changes in the dynamics accompanying the transition throughout the protein have been quantified in terms of the mean-squared fluctuations (MSFs) of methyl hydrogen atoms on the 100 ps time scale. In solution at 300 K the MSFs span a broad distribution, consistent with NMR relaxation measurements. The MSF distribution in the hydrated crystal at 300 K is qualitatively similar to the solution result, except for a slight shift to lower values, and dehydration results in a dramatic shift of the MSFs to lower values. As the temperature is lowered, the whole distribution of methyl group fluctuations in the hydrated crystal shifts to lower values. Most of the methyl groups in the hydrated protein display a nonlinear temperature dependence with a dynamical transition at approximately 200 K, but most methyl groups do not undergo a transition in the dehydrated protein. We conclude that the dynamical transition occurs throughout most of the protein and that solvent is required for the transition.
authors.affiliation: NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA.
authors.forename: Joseph E
authors.initials: JE
authors.lastname: Curtis
authors.forename: Mounir
authors.initials: M
authors.lastname: Tarek
authors.forename: Douglas J
authors.initials: DJ
authors.lastname: Tobias
mesh_terms: D003198:Computer Simulation; D003460:Crystallization; D008958:Models, Molecular; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D012259:Ribonuclease, Pancreatic