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Analysis of hydration of ovalbumin by densitometry was characterised by analysing the excess functions of mixing. This method facilitates the individual evaluation

A study of the excess gibbs energy of ribonuclease a - water mixtures applied to characterize the hydration dependencies of the excess thermodynamic functions of binary protein

Analysis of hydration of binary protein-water mixtures. methodology on the analysis of the excess thermodynamic functions (volume V, enthalpy H, entropy S, heat capacity Cp

Gibbs energies, enthalpies, and entropies of water and lysozyme at the inner edge of excess hydration applied to characterize the hydration dependencies of the excess thermodynamic functions. The excess

A study of the excess gibbs energy of ribonuclease a - water mixtures applied to characterize the hydration dependencies of the excess thermodynamic functions of binary protein

Analysis of hydration of ovalbumin by densitometry was characterised by analysing the excess functions of mixing. This method facilitates the individual evaluation

A study of the heat capacity of ribonuclease a - water mixtures of the excess thermodynamic functions. A major focus of this study aims to show how these thermodynamic

A study of the hydration of ribonuclease A using isothermal calorimetry: Effect of the protein hydrophobicity and polarity to find the excess thermodynamic functions of binary protein-water systems. Isothermal calorimetry

Analysis of hydration of ovalbumin by isothermal calorimetry to characterize the hydration dependencies of the excess thermodynamic functions of binary proteinwater systems

A study of the heat capacity of ribonuclease a - water mixtures of the excess thermodynamic functions. A major focus of this study aims to show how these thermodynamic

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