Solvent denaturation of proteins and interpretations of the m value

The stability of globular proteins is important in medicine, proteomics, and basic research. The conformational stability of the folded state can be determined experimentally by analyzing urea, guanidinium chloride, and thermal denaturation curves. Solvent denaturation curves in particular may give useful information about a protein such as the existence of domains or the presence of stable folding intermediates. The linear extrapolation method (LEM) for analyzing solvent denaturation curves gives the parameter m, which is a measure of the dependence of ΔG on denaturant concentration. There is much recent interest in the m value as it relates to the change in accessible surface area of a protein when it unfolds and what it may reveal about the denatured states of proteins.