Differential Scanning Calorimetry: A Powerful and Versatile Tool for Analyzing Proteins and Peptides

Differential Scanning Calorimetry (DSC) is an efficient and versatile analytical technique widely used to study the thermal properties and stability of proteins. This review article provides a comprehensive overview of the principles and applications of DSC in protein research. DSC measures the heat flow associated with temperature-induced conformational changes in proteins, allowing for the direct determination of key thermodynamic parameters such as melting temperature (Tm), enthalpy change (ΔH), and heat capacity change (ΔCp). These parameters provide valuable insights into protein and peptide stability, folding mechanisms, and interactions with ligands. The review discusses the methodological aspects of DSC, including sample preparation, experimental setup, and data analysis techniques. It also highlights the application of DSC in various aspects, such as drug discovery, biopharmaceutical development, and the study of protein-ligand interactions. By elucidating the thermal behavior of proteins, DSC contributes significantly to our understanding of protein and peptide structure, function, and stability, making it an indispensable tool in biochemical and biophysical research.