鱼精蛋白
DNA
分子
化学
计算生物学
生物物理学
生物
生物化学
有机化学
肝素
作者
Laura H Cree,Rod Balhorn,Laurence R. Brewer
出处
期刊:Protein and Peptide Letters
[Bentham Science Publishers]
日期:2011-08-01
卷期号:18 (8): 802-810
被引量:27
标识
DOI:10.2174/092986611795713943
摘要
Single molecule studies of protamine-DNA interactions have characterized the kinetics of protamine binding to DNA and the morphology of the toroidal subunits that comprise sperm chromatin. The results provided by these studies are reviewed, the advantage of using single molecule techniques is discussed, and the implications of the results to the structure, kinetics of toroid formation, and stability of the DNA-protamine complex are described. New measurements of DNA condensation forces induced by the binding of protamine to DNA are also presented. These forces induce a significant tension in constrained segments of DNA and may contribute to the reduction in volume and shaping of the maturing spermatid cell nucleus.
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