Dynamic force spectroscopy of protein-DNA interactions by unzipping DNA.

by: SJ Koch, MD Wang

Phys Rev Lett, Vol. 91, No. 2. (11 July 2003)

View FullText article

Pubmed, Hubmed

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

TheLarry, skoch3, Koch_Lab (group)

Find related articles with these CiteULike tags

dfs, dna, dynamic, force, no-tag, protein, single-molecule, spectroscopy, ufapa, unzipping

Abstract

We demonstrate the first site-specific single-molecule characterization of the prominent activation barrier for the disruption of a protein-DNA binding complex. We achieved this new capability by combining dynamic force spectroscopy with unzipping force analysis of protein association and used the combination to investigate restriction enzyme binding to specific DNA sites. Analysis revealed lifetimes and interaction distances for three protein-DNA interactions. This new method is able to distinguish protein-DNA binding complexes on a site-specific, single-molecule basis.

@article{citeulike:1085795, abstract = {We demonstrate the first site-specific single-molecule characterization of the prominent activation barrier for the disruption of a protein-DNA binding complex. We achieved this new capability by combining dynamic force spectroscopy with unzipping force analysis of protein association and used the combination to investigate restriction enzyme binding to specific DNA sites. Analysis revealed lifetimes and interaction distances for three protein-DNA interactions. This new method is able to distinguish protein-DNA binding complexes on a site-specific, single-molecule basis.}, address = {Department of Physics, Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, New York 14853, USA.}, author = {Koch, S. J. and Wang, M. D. }, citeulike-article-id = {1085795}, issn = {0031-9007}, journal = {Phys Rev Lett}, month = {July}, number = {2}, posted-at = {2008-05-19 15:43:15}, priority = {3}, title = {Dynamic force spectroscopy of protein-DNA interactions by unzipping DNA.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12906513}, volume = {91}, year = {2003} }

RIS record

TY - JOUR ID - citeulike:1085795 L3 - citeulike-article-id:1085795 TI - Dynamic force spectroscopy of protein-DNA interactions by unzipping DNA. JF - Phys Rev Lett VL - 91 IS - 2 AD - Department of Physics, Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, New York 14853, USA. SN - 0031-9007 N2 - We demonstrate the first site-specific single-molecule characterization of the prominent activation barrier for the disruption of a protein-DNA binding complex. We achieved this new capability by combining dynamic force spectroscopy with unzipping force analysis of protein association and used the combination to investigate restriction enzyme binding to specific DNA sites. Analysis revealed lifetimes and interaction distances for three protein-DNA interactions. This new method is able to distinguish protein-DNA binding complexes on a site-specific, single-molecule basis. AU - Koch, SJ AU - Wang, MD PY - 2003/07/11/ UR - http://view.ncbi.nlm.nih.gov/pubmed/12906513 ER -

RIS BibTeX