Standard state and thermodynamic self-consistency.

It is pointed out that even though the standard state for solutions is a fictitious state, it nonetheless should be thermodynamically self-consistent. Using a volumetric constraint, it is shown that the biochemical standard state concentration of 1M is too high for macromolecules like proteins and nucleic acids that it violates volumetric self-consistency. Also, at 1 M standard state, the mole fraction of these macromolecular solutes is not the commonly held value of 1/55.5, but rather a meaningless negative number. Thus, the ideal mixing entropy (also called cratic entropy) cannot be meaningfully calculated for macromolecules at such a standard state. The relevance of this conclusion to the interpretation of standard bimolecular binding entropy is discussed. Copyright 2001 Wiley-Liss, Inc. and the American Pharmaceutical Association