Discolsing the Role of Hydrophobic Interactions Through Aggregation of non-Polar Solutes in Water: a Molecular Dynamics Study

C. GASTÓN FERRARA; J. RAÚL GRIGERA; OSVALDO CHARA; HUGO ARIEL ALVAREZ

Perugia

Congreso; FRONTIERS IN WATER BIOPHYSICS 2012; 2012

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 Tc and pc. The results are in accordance with previous experimental evidence involving transitions of hydrocarbons in water mixtures, and protein unfolding.