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- W1504021380 abstract "Abstract 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." @default.
- W1504021380 created "2016-06-24" @default.
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- W1504021380 date "2009-12-15" @default.
- W1504021380 modified "2023-10-11" @default.
- W1504021380 title "Probing Biomolecular Interactions Using Nanopore Force Spectroscopy" @default.
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- W1504021380 doi "https://doi.org/10.1002/9780470027318.a9039" @default.
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