THEORY OF REVERSIBLE DENATURATION OF GLOBULAR PROTEINS

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Abstract
A theoretical method is developed by which the character of the process of protein denaturation (e.g., whether or not it is of the all‐or‐none type) can be discussed in terms of conformation of native proteins and the forces stabilizing it. An important role is played by a quantity S(H): entropy of a protein molecule in solution in the conformational states with a given value of enthalpy H. It is demonstrated that the all‐or‐none type denaturation of proteins is a rather direct consequence of the globularity and specificity of the native conformations. Denaturations with significant intermediate states are discussed. Denaturations induced by added denaturants are also discussed.

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