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Measurement of Single Molecular Interactions by Dynamic Force Microscopy

  • Martin Hegner
  • Wilfried Grange
  • Patricia Bertoncini
Part of the Methods in Molecular Biology™ book series (MIMB, volume 242)

Abstract

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).

Keywords

Force Curve Atomic Force Microscope Cantilever Single Molecule Experiment Unbinding Force Bulk Experiment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc., Totowa, NJ 2004

Authors and Affiliations

  • Martin Hegner
    • 1
  • Wilfried Grange
    • 1
  • Patricia Bertoncini
    • 2
  1. 1.NCCR Nanoscale Science, Department of PhysicsUniversity of BaselBaselSwitzerland
  2. 2.Department of Physics, NCCR Nanoscale ScienceUniversity of BaselBaselSwitzerland

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