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 (Figure 1) [1-4]. The burial of hydrophobic regions in a protein's interior, along with the exposure of hydrophilic residues to aqueous solutions stabilizes native structures and ensures solubility. Active native proteins perform their biological functions through highly regulated intermolecular interactions with their binding partners, under thermodynamic control.