Biophysical Application of Calorimetric Methods to Protein Misfolding And Aggregation Examinations

Unfolded proteins fold into thermodynamically-favorable native structures under the correct physiological conditions for gain of function. This whitepaper describes how differential scanning calorimetry and isothermal titration calorimetry can be used as a powerful method for the thermodynamic investigation of interactions between diverse biomolecules and inorganic compounds. It details some examples from literature of the methods application in studying amyloid fibrillation.