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We measure the nonequilibrium binding of a peptide ligand to a phospholipid membrane from isothermal titration calorimetry experiments at high temperature (70 degrees C). The binding isotherm shows signs of multiligand binding and is analyzed within the framework of a rate model that describes the diffusion-controlled binding of peptide from bulk solution to the surface of the lipid membrane. It is shown that the key thermodynamic quantities can be determined from the fitting of the experimental binding isotherms by an appropriate isothermal titration calorimetry model. Specifically, the surface-bound peptide concentration is found from the ratio of the enthalpy and entropy changes associated with binding. In addition, the accessible surface area for binding and the apparent dissociation constant for the binding reaction are obtained. The key parameters are determined by nonlinear regression analysis. The dependence of the calculated rate constants on the surface

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