Solvation thermodynamics of protein studied by the 3D-RISM theory

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DOIResolve DOI: http://doi.org/10.1016/j.cplett.2004.06.140
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TypeArticle
Journal titleChemical Physics Letters
Volume395
Issue1-3
Pages16; # of pages: 6
AbstractThe partial molar volume and the solvation free energy of five globular proteins in aqueous solutions are calculated by the three-dimensional reference interaction site model theory, a modern integral equation theory of molecular liquids. The partial molar volume calculated by the theory shows quantitative agreement with the corresponding experimental data. Concerning the solvation free energy, the theoretical results are compared with estimations by an empirical method which uses the accessible surface area of atoms, because the corresponding experimental data are not available. Possible applications of the method to problems related to the solvation thermodynamics of protein are discussed.
Publication date
AffiliationNational Research Council Canada; National Institute for Nanotechnology
Peer reviewedNo
NPARC number12328241
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Record identifier4e47c58c-0c0e-41f7-a141-e1f5a2bd7598
Record created2009-09-10
Record modified2016-05-09
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