@article {4027,
	title = {{\textquoteright}Intermolecular interactions{\textquoteright} in aqueous solutions of three components including lysozyme},
	journal = {Fluid Phase Equilibria},
	volume = {136},
	number = {1-2},
	year = {1997},
	note = {ISI Document Delivery No.: YR149Times Cited: 5Cited Reference Count: 4614th IUPAC Conference on Chemical Thermodynamics (ICCT 97)AUG 25-30, 1996OSAKA, JAPANInt Union Pure \& Appl Chem, Sci Council Japan, Chem Soc Japan, Japan Soc Calorimetry \& Thermal Anal, Atom Energy Soc Japan},
	month = {Nov},
	pages = {207-221},
	type = {Proceedings Paper},
	abstract = {Excess partial molar enthalpies were measured in ternary aqueous solutions, tert-butyl alcohol (TBA)DMSO-H2O, and lysozyme (L)-alcohols (A)-H2O. The solute-solute interactions were evaluated as the derivatives of these data with respect to the mole fraction of a solute. In the water-rich region, where the so-called mixing scheme I is operating in binary aqueous solutions of TEA, DMSO or alcohols, two solutes in TBA-DMSO-H2O seem to modify the hydrogen bond network of H2O in an additive manner. Here, mixing scheme I refers to the way in which a solute (hydrophobic) modifies the molecular organization of H2O. Specifically, a solute enhances the hydrogen bond strength of H2O in its immediate vicinity. On the other hand, the probability of hydrogen bond in the bulk away from a solute is reduced, and it is still high enough, however, to keep the hydrogen bond network connected throughout the entire macroscopic: system. As the composition of solute increases, the hydrogen bond probability in the bulk decreases to the point at which the macroscopic bond connectivity is no longer possible. At this point, a new mixing scheme, II, sets in. For L-A-H2O mixtures at infinite dilution of L, the L-A interaction changes drastically from repulsive: to attractive at the boundary between I and II for binary aqueous alcohols. Moreover, a denatured lysozyme interacts with alcohols more strongly than the native form, and is more repulsive in mixing scheme I and more attractive in IT. This behaviour is shown to be consistent with the alcohol-dependent enthalpy of denaturation of lysozyme found by Velicelebi and Sturtevant [Velicelebi and Sturtevant, Biochem. 18 (1979) 1188-86]. (C) 1997 Elsevier Science B.V.},
	keywords = {2-BUTOXYETHANOL, BUTYL ALCOHOL, denaturation of lysozyme, enthalpy of, excess partial molar enthalpies, FREE-ENERGIES, HEAT-CAPACITIES, lysozyme-alcohols-H2O, MIXING SCHEME, PARTIAL MOLAR ENTHALPIES, SOLUTE-SOLUTE INTERACTION, TERT-BUTANOL MIXTURES, tert-butyl alcohol-DMSO-H2O, THERMAL EXPANSIVITIES, VAPOR-PRESSURES, WATER-RICH REGION},
	isbn = {0378-3812},
	url = {<Go to ISI>://000071465000020},
	author = {Koga,Yoshikata and Westh, P. and Trandum, C. and Haynes, C. A.}
}
