title: Effect of salt identity on the phase diagram for a globular protein in aqueous electrolyte solution.
abstract: 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. 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.
authors.affiliation: Department of Physics, Chemistry and Biology, Linköping University, SE-581 83, Linköping, Sweden.
authors.forename: Mathias
authors.initials: M
authors.lastname: Boström
authors.forename: Frederico W
authors.initials: FW
authors.lastname: Tavares
authors.forename: Barry W
authors.initials: BW
authors.lastname: Ninham
authors.forename: John M
authors.initials: JM
authors.lastname: Prausnitz
mesh_terms: D003198:Computer Simulation; D004573:Electrolytes / Q000737:chemistry*; D007477:Ions / Q000737:chemistry; D009010:Monte Carlo Method; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D012492:Salts / Q000737:chemistry*; D012996:Solutions
chemical_list: D004573:Electrolytes; D007477:Ions; D012492:Salts; D012996:Solutions; D009113:Muramidase