Isothermal titration calorimetry and differential scanning calorimetry are being used in conjunction with structural methods such as small angle neutron scattering to determine the thermodynamics of protein-protein, protein-DNA, and protein-ligand interactions and conformational changes accompanying these interactions in solutions. Efforts are being made to determine how the initiation of transcription is thermodynamically regulated by transcription activators and repressors for use in gene expression and gene therapy. A differential stopped flow microcalorimetry method is being used for the rapid and universal determination of enzyme kinetic parameters as function of temperature for use in the biocatalyst industry.