Probing Biomolecular Interactions Using Nanopore Force Spectroscopy
Published Online: 15 DEC 2009
Copyright © 2000 John Wiley & Sons, Ltd. All rights reserved.
Encyclopedia of Analytical Chemistry
How to Cite
Dudko, O. K. and Meller, A. 2009. Probing Biomolecular Interactions Using Nanopore Force Spectroscopy. Encyclopedia of Analytical Chemistry. .
- Published Online: 15 DEC 2009
The ability to apply a force on individual biomolecular complexes and measure their time-dependent response have begun to reveal their mechanical properties, interactions with other biomolecules, and self-interactions. A number of single-molecule methods have been developed and applied in the past decade to broad range of biological system, including proteins in the skeletal and cardiac muscle sarcomere, nucleic acid complexes, and enzymes. Nanopore force spectroscopy (NFS) is an emerging single-molecule method that takes advantage of the native electrical charge of biomolecule to exert a localized bond-rupture force. This article reviews the basic principles of the method and discusses two bond-breakage modes utilizing either a constant voltage or a fixed voltage ramp, which are related quantitatively in an essentially model-free way. A unified theoretical formalism is developed to extract kinetic information from the NFS data. The utility of this formalism is illustrated by analyzing data from nanopore unzipping of individual DNA hairpin molecules.
- single-molecule methods;
- nanopore force spectroscopy;
- Kramers theory;
- hairpin unzipping;
- rupture voltage distribution