Binding of TmHU to single dsDNA as observed by optical tweezers
- PMID: 16647714
- DOI: 10.1016/j.jmb.2006.04.006
Binding of TmHU to single dsDNA as observed by optical tweezers
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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