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dc.contributor.authorDahanayake, Jayangika Niroshani
dc.contributor.authorMitchell-Koch, Katie R.
dc.identifier.citationDahanayake, Jayangika Niroshani; Mitchell-Koch, Katie R. 2018. Entropy connects water structure and dynamics in protein hydration layer. Physical Chemistry Chemical Physics. vol. 20:no. 21:pp14765-14777en_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractThe enzyme Candida Antarctica lipase B (CALB) serves here as a model for understanding connections among hydration layer dynamics, solvation shell structure, and protein surface structure. The structure and dynamics of water molecules in the hydration layer were characterized for regions of the CALB surface, divided around each -helix, -sheet, and loop structure. Heterogeneous hydration dynamics were observed around the surface of the enzyme, in line with spectroscopic observations of other proteins. Regional differences in the structure of the biomolecular hydration layer were found to be concomitant with variations in dynamics. In particular, it was seen that regions of higher density exhibit faster water dynamics. This is analogous to the behavior of bulk water, where dynamics (diffusion coefficients) are connected to water structure (density and tetrahedrality) by excess (or pair) entropy, detailed in the Rosenfeld scaling relationship. Additionally, effects of protein surface topology and hydrophobicity on water structure and dynamics were evaluated using multiregression analysis, showing that topology has a somewhat larger effect on hydration layer structure-dynamics. Concave and hydrophobic protein surfaces favor a less dense and more tetrahedral solvation layer, akin to a more ice-like structure, with slower dynamics. Results show that pairwise entropies of local hydration layers, calculated from regional radial distribution functions, scale logarithmically with local hydration dynamics. Thus, the Rosenfeld relationship describes the heterogeneous structure-dynamics of the hydration layer around the enzyme CALB. These findings raise the question of whether this may be a general principle for understanding the structure-dynamics of biomolecular solvation.en_US
dc.description.sponsorshipNational Science Foundation under Grant No. CHE-1665157. This work is also supported by Wichita State University Department of Chemistry and Fairmount College of Liberal Arts and Sciences; the National Science Foundation under Award no. EPS-090 K3806 and matching support from the State of Kansas through the Kansas Board of Regents; and the National Institute of General Medical Sciences (P20 GM103418) from the National Institutes of Health. This work also used the Extreme Science and Engineering Discovery Environment (XSEDE)100 through allocation CHE170093. XSEDE is supported by National Science Foundation grant number ACI-1548562.en_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.ispartofseriesPhysical Chemistry Chemical Physics;v.20:no.21
dc.subjectHydrogen-bond kineticsen_US
dc.subjectUniversal scaling lawen_US
dc.subjectSimple fluidsen_US
dc.subjectLiquid wateren_US
dc.titleEntropy connects water structure and dynamics in protein hydration layeren_US
dc.rights.holder© Royal Society of Chemistry 2018en_US

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