Abstract
The molecular mechanism of the solvent motion that is required to instigate the protein structural relaxation above a critical hydration level or transition temperature has yet to be determined. In this work we use quasi-elastic neutron scattering (QENS) and molecular dynamics simulation to investigate hydration water dynamics near a greatly simplified protein surface. We consider the hydration water dynamics near the completely deuterated N-acetyl-leucine-methylamide (NALMA) solute, a hydrophobic amino acid side chain attached to a polar blocked polypeptide backbone, as a function of concentration between 0.5M-2.0M, under ambient conditions. In this Communication, we focus our results of hydration dynamics near a model protein surface on the issue of how enzymatic activity is restored once a critical hydration level is reached, and provide a hypothesis for the molecular mechanism of the solvent motion that is required to trigger protein structural relaxation when above the hydration transition.
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