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An approach has been proposed to characterize the competitive association ofD2O and to study the heterogeneity of hydration water adsorbed by the protein,immunoglobulin G, using methodology for determining of non-freezing water inmixed H2O-D2O protein solutions by low-temperature 1H NMR technique. Directdata on the numbers of deuteriums adsorbed by immunoglobulin G and isothermalsof water (D2O) sorption by the protein for solution hydration conditions wereobtained. The preferential binding of D2O as well as the isotopic effect of lowD2O concentrations was simply confirmed using this method. The shape of theisothermals, similar to that for polymolecular adsorption, demonstratesrelative changes in the fractions of heavy water isotope bound to differentgroups of protein atoms on decreasing temperature in frozen solution. At -35deg C the major fractions attached to charged and polar atomic groups appear tobe related as 2/3. The adsorption curves indicate the direct relationship ofnon-freezing water to interface water in protein powders.

A Low-temperature 1H NMR Study of H2O and D2O Associated Competitively with Immunoglobulin G in Solution