Heat capacity (C_p) changes are important in understanding the thermodynamics of

• protein folding
• protein-protein binding
• protein-nucleic acid binding
• the hydrophobic effect

Nowadays sensitive and accurate calorimeters provide us with a lot of heat capacity (C_p)data for these processes:

• ITC (Isothermal Titration Calorimetry)- for binding studies
• DSC (Differential Scanning Calorimetry)- for protein folding studies
• PPC (Pressure Perturbation Calorimetry)- for protein volumetric properties studies

Processes that involve changes in C_p can give diverse thermodynamic data as heat capacity relates the other three major thermodynamic quantities:

• enthalpy (H)
• entropy (S)
• free energy (G)

Changes in C_p associated with protein folding and binding come mostly from changes in hydration that are due to burial of polar and nonpolar groups in protein interior.

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Last updated on 20 November 2001