Thermodynamic investigations of proteins. I. Standard functions for proteins with lysozyme as an example.
A direct method is proposed for obtaining thermodynamic standard functions for native and denatured proteins using experimental data from scanning calorimetry, isothermal calorimetry and potentiometric titrations. The possibility of this approach is demonstrated on the example of lysozyme in the range of pH 1.5-7.0 and temperature 0-100 degrees C. Tests for the validity of the obtained functions of enthalpy and entropy are presented in the form of cyclic processes using experimental data obtained from thermodynamically different pathways. The Gibbs function is checked by comparison with results of an independent method. The methodic problems in determining and checking standard functions for proteins are discussed in detail.
D002151:Calorimetry; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D009113:Muramidase; D011199:Potentiometry; D011489:Protein Denaturation; D011506:Proteins; D013696:Temperature; D013816:Thermodynamics
D011506:Proteins; D009113:Muramidase