An enthalpic approach to the analysis of the scanning force ligand rupture experiment

Abstract

The scanning force microscope has developed into a technique for the examination of key events involved in molecular interactions. Here we present a novel method to analyse the new family of force data obtained from this biophysical tool. Adiabatic mapping of the streptavidin–biotin interaction reveals a range of ligand rupture forces from 253 to 393 pN, which are in close agreement with experimental data. Analysis of the undocking process shows the importance of hydrogen bonding in this interaction. The potential of this combined approach as a method of studying rupture force data is highlighted.

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