Abstract
We report, for the first time, the application of multidimensional cross-correlation relaxometry to a model globular aqueous protein system (bovine serum albumin) over a wide range of water contents from the solution to glassy states. Off-diagonal cross-relaxation peaks are observed and lend support to the proton-exchange cross-relaxation model of water relaxation. The dependence of the water proton relaxation rates on water content is also consistent with the multistate theory of water dynamics in protein systems. Evidence for water compartmentation in bovine serum albumin gels is presented and the potential of multidimensional cross-correlation nuclear magnetic resonance relaxometry in elucidating water–biopolymer interactions in more complex heterogeneous biopolymer systems is discussed.
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