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  Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium

Barnes, R., Sun, S., Fichou, Y., Dahlquist, F. W., Heyden, M., & Han, S. (2017). Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium. Journal of the American Chemical Society, 139(49), 17890-17901. doi:10.1021/jacs.7b08606.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-FC7B-B Version Permalink: http://hdl.handle.net/21.11116/0000-0000-FC7C-A
Genre: Journal Article

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 Creators:
Barnes, Ryan1, Author
Sun, Sheng1, Author
Fichou, Yann1, Author
Dahlquist, Frederick W.1, Author
Heyden, Matthias2, 3, Author              
Han, Songi1, 4, Author
Affiliations:
1 Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, California 93106, United States, ou_persistent22              
2Research Group Heyden, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1950292              
3School of Molecular Sciences, Arizona State University, Tempe, Arizona 85281, United States, ou_persistent22              
4Department of Chemical Engineering, University of California, Santa Barbara, Santa Barbara, California 93106, United States, ou_persistent22              

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 Abstract: Hydration water on the surface of a protein is thought to mediate the thermodynamics of protein–ligand interactions. For hydration water to play a role beyond modulating global protein solubility or stability, the thermodynamic properties of hydration water must reflect on the properties of the heterogeneous protein surface and thus spatially vary over the protein surface. A potent read-out of local variations in thermodynamic properties of hydration water is its equilibrium dynamics spanning picosecond to nanosecond time scales. In this study, we employ Overhauser dynamic nuclear polarization (ODNP) to probe the equilibrium hydration water dynamics at select sites on the surface of Chemotaxis Y (CheY) in dilute solution. ODNP reports on site-specific hydration water dynamics within 5–10 Å of a label tethered to the biomolecular surface on two separate time scales of motion, corresponding to diffusive water (DW) and protein–water coupled motions, referred to as bound water (BW). We find DW dynamics to be highly heterogeneous across the surface of CheY. We identify a significant correlation between DW dynamics and the local hydropathy of the CheY protein surface, empirically determined by molecular dynamics (MD) simulations, and find the more hydrophobic sites to be hydrated with slower diffusing water. Furthermore, we compare the hydration water dynamics on different polypeptides and liposome surfaces and find the DW dynamics on globular proteins to be significantly more heterogeneous than on intrinsically disordered proteins (IDPs), peptides, and liposomes. The heterogeneity in the hydration water dynamics suggests that structured proteins have the capacity to encode information into the surrounding hydration shell.

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Language(s): eng - English
 Dates: 2017-08-132017-11-012017-12-13
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.7b08606
 Degree: -

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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 139 (49) Sequence Number: - Start / End Page: 17890 - 17901 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870