Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and of hydrostatic pressure.
The native conformation of oligomers may be expected to undergo reversible changes when they separate upon dissociation of the original aggregate. When these changes are slow in comparison with the time of an association-dissociation (AD) cycle, they give rise to characteristic effects in the dependence of the dissociation: upon dilution, at constant pressure, and upon the applied pressure, at constant concentration. The phenomenological description of these effects is examined by comparing two possible models: The first model assumes a continuous loss in free energy of association with the extent of dissociation; the second supposes the existence of two or more distinct aggregates differing in subunit affinity and present in proportions that vary with the extent of dissociation. The latter model fits better the experimental data available, with regard to both the concentration and the pressure dependence of the association, and gives a particularly simple explanation of the hysteresis phenomena observed in several oligomeric proteins after application of pressure. The validity of the principle of detailed balance, often assumed in dealing with complex equilibria, is discussed in detail as it does not appear possible to reconcile it with some of the experimental observations or with the proposed model.
D006874:Hydrostatic Pressure; D007700:Kinetics; D046911:Macromolecular Substances; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics
D046911:Macromolecular Substances; D011506:Proteins