Abstract
The thermodynamic properties of aqueous globular proteins are considered, both when at equilibrium in a heat bath and during enzymatic catalysis. It is recognized that they exhibit thermally driven conformational fluctuations of great complexity and on time scales that may be much faster than the enzyme turnover time. Yet conformational states of proteins can store free energy under macroscopically isothermal conditions. This requires that they possess special, collective, non-thermally excited modes both during enzymatic catalysis and, in particular, during free energy conservation. Electron transport phosphorylation and related membrane processes provide well-defined examples of this latter behavior.
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