@article {2218,
	title = {Hydrophobic interactions in urea - Trimethylamine-N-oxide solutions},
	journal = {Journal of Physical Chemistry B},
	volume = {112},
	number = {35},
	year = {2008},
	note = {ISI Document Delivery No.: 342RDTimes Cited: 2Cited Reference Count: 25Paul, Sandip Patey, G. N.},
	month = {Sep},
	pages = {11106-11111},
	type = {Article},
	abstract = {The influence of osmolytes urea and trimethylemine-N-oxide (TMAO) on hydrophobic interactions is investigated employing molecular dynamics simulations. These osmolytes are of interest because of their opposing influence on proteins in solution; the denaturing effect of urea can be countered with TMAO. A neopentane pair is used to model typical nonpolar entities. Binary water-urea and water-TMAO as well as ternary water-urea-TMAO systems are considered. Neopentane-neopentane potentials of mean force, neopentane-water, and neopentane-osmolyte distribution functions are reported. Urea is found to have only modest influence on the neopentane-neopentane potential of mean force, but the hydrophobic attraction is completely destroyed by the presence of TMAO. It is shown that TMAO tends to act as a simple "surfactant" displacing water and urea (if it is present) from the first solvation shell of neopentane. It is likely the surfactant-like influence of TMAO that accounts for the elimination of the hydrophobic attraction. The implications of Our results for explanations of the action of TMAO in protein solutions are discussed.},
	keywords = {AQUEOUS UREA, FORCE, MOLECULAR-DYNAMICS, OSMOLYTES, POTENTIALS, PROTEIN DENATURATION, SIMULATIONS, WATER},
	isbn = {1520-6106},
	url = {<Go to ISI>://000258800300046},
	author = {Paul, S. and Patey, G. N.}
}
