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Influence of Hydration on the Dynamics of Lysozyme

J. H. Roh ^*, J. E. Curtis , S. Azzam , V. N. Novikov ^*, I. Peral , Z. Chowdhuri , R. B. Gregory  and A. P. Sokolov ^*

^* Department of Polymer Science, The University of Akron, Akron, Ohio; National Institute of Standards and Technology, Gaithersburg, Maryland; and Department of Chemistry, Kent State University, Kent, Ohio

Correspondence: Address reprint requests to Alexei P. Sokolov, Dept. of Polymer Science, The University of Akron, Akron, OH 44325-3909. E-mail: alexei{at}uakron.edu.

Quasielastic neutron and light-scattering techniques along with molecular dynamics simulations were employed to study the influence of hydration on the internal dynamics of lysozyme. We identified three major relaxation processes that contribute to the observed dynamics in the picosecond to nanosecond time range: 1), fluctuations of methyl groups; 2), fast picosecond relaxation; and 3), a slow relaxation process. A low-temperature onset of anharmonicity at T 100 K is ascribed to methyl-group dynamics that is not sensitive to hydration level. The increase of hydration level seems to first increase the fast relaxation process and then activate the slow relaxation process at h 0.2. The quasielastic scattering intensity associated with the slow process increases sharply with an increase of hydration to above h 0.2. Activation of the slow process is responsible for the dynamical transition at T 200 K. The dependence of the slow process on hydration correlates with the hydration dependence of the enzymatic activity of lysozyme, whereas the dependence of the fast process seems to correlate with the hydration dependence of hydrogen exchange of lysozyme.

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