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
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