4.8 Article

Single-molecule analysis of DNA-protein complexes using nanopores

Journal

NATURE METHODS
Volume 4, Issue 4, Pages 315-317

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH1021

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Funding

  1. NHGRI NIH HHS [HG003703] Funding Source: Medline
  2. NIGMS NIH HHS [GM075893] Funding Source: Medline

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We present a method for rapid measurement of DNA-protein interactions using voltage-driven threading of single DNA molecules through a protein nanopore. Electrical force applied to individual ssDNA-exonuclease I complexes pulls the two molecules apart, while ion current probes the dissociation rate of the complex. Nanopore force spectroscopy (NFS) reveals energy barriers affecting complex dissociation. This method can be applied to other nucleic acid-protein complexes, using protein or solid-state nanopore devices.

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