Abstract
How much information is required to evaluate the equilibrium constants of structural changes in biopolymers. Hemoglobin structures are known in great detail, but their complexity limits our ability to extract information about the energetics of interaction in solution and the equilibria involving structural changes. We have found that it is possible to account for a number of aspects of hemoglobin equilibria by minimizing detail and using only two molecular parameters, the surface area and the surface charge. The surface area, the interfacial contact area between the molecule and the solution, can be estimated from x-ray structures while the surface charge can be calculated from titration data. In this brief presentation we shall outline our general approach and some results of our calculations. It appears that the two molecular parameters, when combined to evaluate a surface free energy, provide enough detail for physically meaningful energy calculations.
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