Turner, Matthew S. (2000) Two time constants for the binding of proteins to DNA from micromechanical data. Biophysical Journal, Vol.78 (No.2). pp. 600-607. doi:10.1016/S0006-3495(00)76620-3

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Abstract

Recent experimental advances allow the direct measurement of the force/extension behavior for DNA in the presence of strongly binding proteins. Such experiments reveal information about the cooperative mechanism of protein binding. We have studied the irreversible binding of such proteins to DNA using a simple simulation and present a method for estimating quantitative rate constants for the nucleation and growth of linear domains of proteins bound to DNA. Such rate constants also give information about the relative energetics of the two binding processes. We discuss our results in the context of recent data for the DNA-recA-ATPγs system, for which the nucleation time is 4.7 × 104 min per recA binding site and the total growth rate of each domain is 1400 recA/min.

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH426 Genetics Q Science > QC Physics
Divisions:	Faculty of Science > Physics
Library of Congress Subject Headings (LCSH):	Protein binding, DNA-ligand interactions, Nucleation
Journal or Publication Title:	Biophysical Journal
Publisher:	Biophysical Society
ISSN:	0006-3495
Official Date:	February 2000
Dates:	Date Event February 2000 Published
Volume:	Vol.78
Number:	No.2
Page Range:	pp. 600-607
DOI:	10.1016/S0006-3495(00)76620-3
Status:	Peer Reviewed
Access rights to Published version:	Open Access
Funder:	Royal Society (Great Britain), W. M. Keck Foundation, Burroughs Wellcome Fund (BWF)

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