Binding of TmHU to single dsDNA as observed by optical tweezers

Journal of Molecular Biology
Mathias SalomoFriedrich Kremer

Abstract

Optical tweezers are employed to study the action of the histone-like protein from Thermotoga maritima (TmHU) on DNA at a single molecule level. Binding and disruption of TmHU to and from DNA are found to take place in discrete steps of 4-5 nm length and a net binding enthalpy of about 16kBT. This is in reasonable agreement with a microscopic model that estimates the extension of the binding sites of the protein and evaluates the energetics mainly for bending of the DNA in the course of interaction.

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Citations

Apr 2, 2008·European Biophysics Journal : EBJ·Mathias SalomoFriedrich Kremer
Jan 3, 2012·Journal of Biological Physics·Carolin WagnerFriedrich Kremer
Mar 10, 2011·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Paul LiebesnyLaura Finzi
Jun 26, 2010·Physics of Life Reviews·Kathy R ChaurasiyaMark C Williams
Jan 28, 2009·Biosensors & Bioelectronics·L J SteinbockU F Keyser
Oct 30, 2007·Journal of Molecular Biology·Micah J McCauleyMark C Williams
Jul 31, 2007·Microscopy Research and Technique·Mathias SalomoFriedrich Kremer
Apr 22, 2011·Journal of Physics. Condensed Matter : an Institute of Physics Journal·C GutscheF Kremer
Sep 4, 2008·Physical Review Letters·S M Rappaport, Y Rabin
Mar 16, 2007·Physical Review Letters·K KeglerF Kremer

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