Determination of Binding Constants and Related Parameters

To illustrate how binding constants may be evaluated from halide NMR experiments we will make the assumption that there are present on the macromolecule only two classes of halide ion binding sites, B and C, characterized by the binding constants Kg(X) and K (X) for the halide ion X. We will furthermore assume that there are n binding sites of 

An excellent treatise of multiple equilibria in proteins has been presented by Steinhardt and Reynolds [414]. Their ideas have recently been utilized by Nome et al. in the case of serum albumin [252] and we will here mainly follow their treatment. 

We can infer from Eq. (8,42) that the excess relaxation rates 

A (t ) as well as the excess line width, Av, should be directly pro- 1 e 

If we assume Lorentzian line shape for the halide ion NMR signal we have Av = (ttT2) , where Av is the line width at half height. 

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