Description of Hydration Water in Protein (Green Fluorescent Protein) Solution

Perticaroli, Stefania; Ehlers, Georg; Stanley, Christopher B.; Mamontov, Eugene; O’Neill, Hugh; Zhang, Qiu; Cheng, Xiaolin; Myles, Dean A. A.; Katsaras, John; Nickels, Jonathan D.

doi:10.1021/jacs.6b08845

Title: Description of Hydration Water in Protein (Green Fluorescent Protein) Solution

Journal Article · Wed Oct 26 00:00:00 EDT 2016 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/jacs.6b08845· OSTI ID:1341561

Perticaroli, Stefania ^[1]; Ehlers, Georg ^[2]; Stanley, Christopher B. ^[3]; Mamontov, Eugene ^[4]; O’Neill, Hugh ^[3]; Zhang, Qiu ^[3]; Cheng, Xiaolin ^[5]; Myles, Dean A. A. ^[3]; Katsaras, John ^[1]; Nickels, Jonathan D. ^[1]

Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Shull Wollan Center and Biology and Soft Matter Division
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Quantum Condensed Matter Division
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Biology and Soft Matter Division
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Chemical and Engineering Materials Division
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Molecular Biophysics

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. Here, we present an experimental description of the dynamical perturbation of hydration water around green fluorescent protein in solution. Less than two shells (~5.5 Å) 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. Furthermore, this dependence on probe length demonstrates that hydration water undergoes subdiffusive motions (τ ∝ q^–2.5for the first hydration shell, τ ∝ q^–2.3 for perturbed water in the second shell), an important difference with neat water, which demonstrates diffusive behavior (τ ∝ q^–2). Our 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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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1341561

Journal Information:: Journal of the American Chemical Society, Vol. 139, Issue 3; ISSN 0002-7863

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 60 works

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