RESUMEN
Water in protein/water mixtures can be described in terms of bound water and free water, by exchange between these two states, and by its exchange with appropriate sites on the protein. 1H-NMR diffusion and relaxation measurements provide insights into the mobility of these states. T2 relaxation-time dispersions (i.e., T2 relaxation times at different echo pulse spacings) reveal additional information about exchange. We present a comprehensive set of diffusion and T2 dispersion measurements on casein gels for which the protein/water ratio ranges from 0.25 to 0.5. The combination of these methods, taken in conjunction with concentration dependence, allows a good estimate of the parameters required to fit the data with Luz/Meiboom and Carver/Richards models for relaxation and chemical exchange. We compare the exchange (a) between water and protein and (b) between free water and bound water. Further, we attempt to distinguish chemical site exchange and diffusion/susceptibility exchange.