Journal
NATURE METHODS
Volume 4, Issue 4, Pages 315-317Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH1021
Keywords
-
Categories
Funding
- NHGRI NIH HHS [HG003703] Funding Source: Medline
- NIGMS NIH HHS [GM075893] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available