Differential scanning calorimetry (DSC) to analyze stability of biomolecules (CAT#: STEM-MB-0237-WXH)

Introduction

Differential Scanning Calorimetry is an analytical technique used to directly characterize the stability of native proteins or other biomolecules. It does this by measuring the thermal changes associated with thermal denaturation of molecules when heated at a constant rate.
Biomolecules in solution are in equilibrium between their native (folded) and denatured (unfolded) conformations. The higher the thermal transition point (Tm), the more stable the molecule. DSC measures the enthalpy of unfolding (H) caused by heat-induced denaturation. It is also used to determine the change of heat capacity of denaturation (Cp). Differential scanning calorimetry can elucidate factors that affect the folding and stability of native biomolecules. These include hydrophobic interactions, hydrogen bonding, conformational entropy and physical environment.