Thermodynamic linkage of ion binding and hydration in myofibrillar protein solutions determined from multinuclear spin relaxation studies

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Macromolecular Symposia


The mechanisms for the anionic and cationic interactions with myofibrillar proteins in aqueous solutions were investigated by nuclear magnetic resonance over a wide range of salt concentration. Markedly nonlinear dependeces of the 17O and 23Na NMR transverse relaxation rates on salt concentration were analyzed with a thermodynamic linkage model of salt-dependent solubility and hydration (ligand-induced association model), according to Wyman's theory of linked functions. Nonlinear regression analysis of both 17O and 23Na NMR data suggested cooperative, reversible binding of hydrated ions to myofibrillar proteins. Both ions and water were found to exchange fast, on the NMR timescale, between the binding sites of the myofibrillar proteins and the aqueous solution. At sodium chloride concentrations higher than about 0.1 grams salt/gram water, ion activities have marked effects upon the NMR relaxation rates of both ions and water. A salt activity model allowed quantitative fitting of the NMR data at high salt concentrations. The effect of neglecting the ion activity in solutions of myofibrillar proteins was also estimated and compared with the ligand-induced, cooperative association model for myofibrillar proteins. The comparison between the 17O and 23Na results strongly suggests that water is exchanged as the hydrated ion species between the myofibrillar protein binding sites and the bulk, aqueous solution.

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