THEORY OF LARGE‐AMPLITUDE CONFORMATIONAL FLUCTUATIONS IN NATIVE GLOBULAR PROTEINS. Independent Fluctuating Site Model

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<jats:p>A theory is developed about large‐amplitude conformational fluctuations in globular proteins in their native or predenaturational state. A model is introduced, an independent fluctuating site model, in which we assume that there is more than one independent fluctuating site, each one localized in some part of a protein molecule. Without assuming any further details for each fluctuating site, the entropy S versus enthalpy H curve of this model is shown to be convex. From this fact the predenaturational excess heat capacity can be derived, as observed in recent experimental studies of a few systems of a protein in solution.</jats:p>

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