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    Crucial Importance of Water Structure Modification on Trimethylamine N-Oxide Counteracting Effect at High Pressure
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    Department of Chemistry, Indian Institute of Technology, Guwahati Assam, India-781039
    *Electronic address: [email protected]
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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2013, 117, 2, 677–689
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    https://doi.org/10.1021/jp311102v
    Published December 27, 2012
    Copyright © 2012 American Chemical Society
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    Abstract

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    Penetration of water molecules into the protein interior under high hydrostatic pressure conditions, leading to protein structural transition, is a well-known phenomenon. The counteracting effect of a naturally occurring osmolyte, trimethylamine N-oxide (TMAO), against pressure-induced protein denaturation is also well-established. But, what is largely unknown is the mechanism by which TMAO counteracts this protein denaturation. So to provide a molecular level understanding of how TMAO protects proteins at high pressure, we report here molecular dynamics (MD) computer simulation results for aqueous solutions of N-methylacetamide (NMA) with different TMAO concentrations over a wide range of pressures relevant to protein denaturation. Hydration behavior of NMA is analyzed at different conditions chosen. It is observed that hydrostatic pressure leads to a significant compression of hydration shell of nonpolar groups and increases hydration number. The compression is relatively insignificant in the vicinity of hydrogen bonding sites. TMAO can prevent pressure-induced enhanced hydration of NMA molecules. Interaction of TMAO with NMA and the structural and dynamical properties of water (site–site radial distribution function, coordination number, hydrogen-bond number, and lifetime) are also investigated to find the origin of the counteracting action of TMAO. Our results confirm that TMAO and pressure have counteracting effects on the water structural and dynamical properties, giving an explanation as to how TMAO counteracts pressure-conferred denaturation of proteins.

    Copyright © 2012 American Chemical Society

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    Supporting Information

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    NMA–NMA and NMA–TMAO hydrogen bond number as a function of pressure as well as of TMAO concentration. TMAO carbon–water oxygen and TMAO oxygen–water hydrogen site–site rdfs. TMAO–water hydrogen bond number per TMAO oxygen. This information is available free of charge via the Internet at http://pubs.acs.org.

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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2013, 117, 2, 677–689
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jp311102v
    Published December 27, 2012
    Copyright © 2012 American Chemical Society
    Request reuse permissions

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