Measurement of Single Molecular Interactions by Dynamic Force Microscopy
Unbinding forces of weak, noncovalent bonds have been measured by scanning force microscopy (1) or biomembrane force probes (2). Initially, these scanning force microscopy measurements focused on feasibility studies to measure single biomolecular interactions (3, 4, 5). Recently, however, a few groups showed that these single molecule experiments give a direct link to bulk experiments where thermodynamic data are experimentally acquired (6, 7, 8, 9). In contrast with bulk experiments where averaged properties are measured, a single molecular approach gives access to properties that are hidden in the ensemble. These experiments can give insight into the geometry of the energy landscape of a biomolecular bond (7,9, 10, 11). Some experiments even showed that intermediate states during unbinding (unfolding) exist which only can be detected by single molecule experiments (12, 13, 14).
KeywordsForce Curve Atomic Force Microscope Cantilever Single Molecule Experiment Unbinding Force Bulk Experiment
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