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Effect of Salt Identity on the Phase Diagram for a Globular Protein in aqueous Electolyte Solution

Bostrom, Mathias Anders; Tavares, Frederico W; Ninham, Barry; Prausnitz , John M

Description

Monte Carlo simulations are used to establish the potential of mean force between two globular proteins in an aqueous electrolyte solution. This potential includes nonelectrostatic contributions arising from dispersion forces first, between the globular proteins, and second, between ions in solution and between each ion and the globular protein. These latter contributions are missing from standard models. The potential of mean force, obtained from simulation, is fitted to an analytic equation....[Show more]

dc.contributor.authorBostrom, Mathias Anders
dc.contributor.authorTavares, Frederico W
dc.contributor.authorNinham, Barry
dc.contributor.authorPrausnitz , John M
dc.date.accessioned2015-12-08T22:16:22Z
dc.identifier.issn1520-6106
dc.identifier.urihttp://hdl.handle.net/1885/30640
dc.description.abstractMonte Carlo simulations are used to establish the potential of mean force between two globular proteins in an aqueous electrolyte solution. This potential includes nonelectrostatic contributions arising from dispersion forces first, between the globular proteins, and second, between ions in solution and between each ion and the globular protein. These latter contributions are missing from standard models. The potential of mean force, obtained from simulation, is fitted to an analytic equation. Using our analytic potential of mean force and Barker-Henderson perturbation theory, we obtain phase diagrams for lysozyme solutions that include stable and metastable fluid-fluid and solid-fluid phases when the electrolyte is 0.2 M NaSCN or NaI or NaCl. The nature of the electrolyte has a significant effect on the phase diagram.
dc.publisherAmerican Chemical Society
dc.sourceJournal of Physical Chemistry B
dc.subjectKeywords: Barker-Henderson perturbation theory; Dispersion forces; Computer simulation; Dispersions; Electrolytes; Mathematical models; Phase diagrams; Solutions; Proteins; electrolyte; inorganic salt; ion; lysozyme; article; chemistry; computer simulation; metabol
dc.titleEffect of Salt Identity on the Phase Diagram for a Globular Protein in aqueous Electolyte Solution
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume110
dc.date.issued2007
local.identifier.absfor010501 - Algebraic Structures in Mathematical Physics
local.identifier.ariespublicationu9210271xPUB75
local.type.statusPublished Version
local.contributor.affiliationBostrom, Mathias Anders, Linkoping University
local.contributor.affiliationTavares, Frederico W, Universidade Federal do Rio de Janeiro
local.contributor.affiliationNinham, Barry, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationPrausnitz , John M, University of California
local.description.embargo2037-12-31
local.bibliographicCitation.startpage24757
local.bibliographicCitation.lastpage24760
local.identifier.doi10.1021/jp061191g
dc.date.updated2015-12-08T08:00:41Z
local.identifier.scopusID2-s2.0-33846061271
CollectionsANU Research Publications

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