In molecular recognition force microscopy (MRFM), ligands are covalently attached to atomic force microscopy tips for the molecular recognition of their cognitive receptors on probe surfaces. A ligand-containing tip is approached towards the receptors on the probe surface, which possibly leads to formation of a receptor-ligand bond. The tip is subsequently retracted until the bond breaks at a certain force (unbinding force). In force spectroscopy (FS), the dynamics of the experiment is varied, which reveals a logarithmic dependence of the unbinding force from the loading rate. These studies give insight into the molecular dynamics of the receptor-ligand recognition process and yield information about the binding pocket, binding energy barriers, and kinetic reaction rates. Applications on isolated proteins, native membranes, viruses, and cells will be presented. We have also developed a method for the localization of specific binding sites and epitopes with nm positional accuracy. A magnetically driven AFM tip containing a ligand covalently bound via a tether molecule is oscillated at a few nm amplitude while scanning along the surface. In this way, topography and recognition images are obtained simultaneously.
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