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    • Keywords


      Hydration of myosin; thermodynamics of binding; Water-solute binding

    • Abstract


      From the isopiestic measurements of the extents of adsorption of water vapour by fish myosin at various values of water activities at three different temperatures, the changes in free energy, enthalpy and entropy of dehydration of the protein have been calculated. Extents of excess binding of solvent and solute to myosin have also been determined from isopiestic experiments in the presence of different inorganic salts, sucrose and urea respectively. Mols of water and solute respectively bound in absolute amounts to myosin have been evaluated from these data in limited range of solute concentrations. Free energy changes at different concentrations of these solutes have also been evaluated and their relations with ‘salting-in’ and ‘salting-out’ phenomena have been discussed. The order of the values of the standard free energy change for excess binding calculated with respect to an unified thermodynamic scale are found to be consistent with relative reactivity of binding water to myosin in the presence of inorganic salts, sucrose and urea.

    • Author Affiliations


      Madhusweta Das1 D K Chattoraj1

      1. Department of Food Technology and Biochemical Engineering, Jadavpur University, Calcutta - 700 032, India
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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