通过光镊观察到的TmHU与单链双链DNA的结合。
Binding of TmHU to single dsDNA as observed by optical tweezers.
作者信息
Salomo M, Kroy K, Kegler K, Gutsche C, Struhalla M, Reinmuth J, Skokov W, Immisch C, Hahn U, Kremer F
机构信息
Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, Brüderstrasse 34, D-04103 Leipzig, Germany.
出版信息
J Mol Biol. 2006 Jun 9;359(3):769-76. doi: 10.1016/j.jmb.2006.04.006. Epub 2006 Apr 19.
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.
利用光镊在单分子水平上研究来自嗜热栖热菌（TmHU）的组蛋白样蛋白对DNA的作用。发现TmHU与DNA的结合和解离以4-5纳米长度的离散步骤发生，净结合焓约为16kBT。这与一个微观模型合理吻合，该模型估计了蛋白质结合位点的延伸，并主要评估了相互作用过程中DNA弯曲的能量学。
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