Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2189693 | Journal of Molecular Biology | 2006 | 8 Pages |
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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Authors
M. Salomo, K. Kroy, K. Kegler, C. Gutsche, M. Struhalla, J. Reinmuth, W. Skokov, C. Immisch, U. Hahn, F. Kremer,