Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 3, Pages 1098-1105Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b08845
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Funding
- Center for Structural Molecular Biology - DOE Office of Biological and Environmental Research [FWP ERKP291]
- Scientific User Facilities Division, Office of Basic Energy Sciences, DOE
- U.S. Department of Energy [DEAC0500OR22725]
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The structurally and dynamically perturbed hydration shells that surround proteins and biomolecules have a substantial influence upon their function and stability. This makes the extent and degree of water perturbation of practical interest for general biological study and industrial formulation. We present an experimental description of the dynamical perturbation of hydration water around green fluorescent protein in solution. Less than two shells (similar to 5.5 angstrom) were perturbed, with dynamics a factor of 2-10 times slower than bulk water, depending on their distance from the protein surface and the probe length of the measurement. This dependence on probe length demonstrates that hydration water undergoes subdiffusive motions (tau proportional to q(-2.5) for the first hydration Shell, tau proportional to q(-2.3) for perturbed water in the second shell), an important difference with neat water, which demonstrates diffusive behavior (tau proportional to q(-2)). These results help clarify the seemingly conflicting range of values reported for hydration water retardation as a logical consequence of the different length scales probed by the analytical techniques used.
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