特定蛋白质 - DNA 相互作用的各个方面；寡肽抗生素纺锤菌素与富含（A.T）的 DNA 片段的多模式结合。
Aspects of specific protein-DNA interaction; multi-mode binding of the oligopeptide antibiotic netropsin to (A.T)-rich DNA segments.
作者信息
Reinert K E, Stutter E, Schweiss H
出版信息
Nucleic Acids Res. 1979 Nov 10;7(5):1375-92. doi: 10.1093/nar/7.5.1375.
Abstract
By means of titration viscometry a number of distinct modes could be resolved for the interaction between the antibiotic netropsin and DNA species of 50, 58, and 69 mole + (A+T) below r = 0.04 netropsin molecules bound per DNA phosphate group. The number of corresponding binding sites increases with a high power of the (A+T) content. The apparent association constants are very high (greater than 10(6) M-1, some perhaps greater than 10(6) M-1) and also rather different for most of the binding sites. It is suggested that some of these interaction modes differ in the number of hydrogen bonds formed between donors of the ligand and acceptors of the binding sites. The interaction modes were characterized quantitatively by their (species-independent) changes of DNA contour length and by the percentage of local DNA stiffening.
摘要
通过滴定粘度法，在每个DNA磷酸基团结合的诺托品分子数r = 0.04以下，可分辨出抗生素诺托品与50、58和69摩尔% + (A+T)的DNA物种之间相互作用的多种不同模式。相应结合位点的数量随(A+T)含量的高次方增加。表观缔合常数非常高（大于10⁶ M⁻¹，有些可能大于10⁹ M⁻¹），并且大多数结合位点的表观缔合常数也有相当大差异。有人提出，这些相互作用模式中的一些在配体供体与结合位点受体之间形成的氢键数量上有所不同。通过DNA轮廓长度的（与物种无关的）变化以及局部DNA变硬的百分比对相互作用模式进行了定量表征。
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