Protein-Water Interactions from 2H NMR Relaxation Studies: Influence of Hydrophilic, Hydrophobic, and Electrostatic Interactions
Part of the
Advances in Experimental Medicine and Biology
book series (AEMB, volume 302)
The importance of water interactions with proteins in food systems is well documented. A controversy exists, however, as to the nature of these interactions and the effect of protein structural changes on them. To clarify these questions, a method has been developed for determining hydration from the protein concentration-dependence of deuteron resonance relaxation rates. Measurements were made in D2O on β-lactoglobulin A to study effects of hydrophilic interactions, and on both casein micelles and submicelles to study hydrophobic and electrostatic effects. From the protein concentration-dependent relaxation rates, the second virial coefficients of the proteins were obtained by nonlinear regression analysis. Using either an isotropic tumbling or an intermediate asymmetry model, hydrations, ν̄, and correlation times, τc, were calculated for the protein-associated water; from τc, the Stokes radius, R, was obtained. Variations in ν̄ and R were in accord with known structural changes in molecular states of the proteins. The NMR results are compared with hydrations and structural information derived independently from small-angle X-ray scattering.
KeywordsNuclear Magnetic Resonance Relaxation Rate Virial Coefficient Casein Micelle Nuclear Magnetic Resonance Experiment
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