title: Aggregation of non-polar solutes in water at different pressures and temperatures: the role of hydrophobic interaction.
abstract: Due to the importance of the hydrophobic interaction in protein folding, we decided to study the effect of pressure and temperature on the phase transitions of non-polar solutes in water, and thereby their solubility, using molecular dynamics simulations. The main results are: (1) within a certain range, temperature induces the aggregation of Lennard-Jones particles in water; and (2) pressure induces disaggregation of the formed clusters. From the simulated data, a non-monotonic coexistence curve for the binary system was obtained, from which a critical point of T(c) = 383 ± 9 K and p(c) = 937 ± 11 bar was determined. The results are in accordance with previous experimental evidence involving transitions of hydrocarbons in water mixtures, and protein unfolding.
authors.affiliation: Instituto de Física de Líquidos y Sistemas Biológicos (IFLYSIB) CONICET-UNLP, 59-789, B1900 La Plata, Argentina. gferrara72@gmail.com
authors.forename: C Gastón
authors.initials: CG
authors.lastname: Ferrara
authors.forename: Osvaldo
authors.initials: O
authors.lastname: Chara
authors.forename: J Raúl
authors.initials: JR
authors.lastname: Grigera
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D011312:Pressure; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D013696:Temperature; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D014867:Water