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大肠杆菌DNA解旋蛋白与单链DNA协同结合的研究。

Studies on the cooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA.

作者信息

Ruyechan W T, Wetmur J G

出版信息

Biochemistry. 1975 Dec 16;14(25):5529-34. doi: 10.1021/bi00696a023.

DOI:10.1021/bi00696a023
PMID:1103970
Abstract

The cooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA has been studied by electron microscopy. Analysis of the electron microscopic data by means of a simple statistical mechanical model has yielded a value of 3.8-7.6 X 10(10) l./mol for the cooperative binding constant in 0.15 M NaCl. Studied under elevated salt conditions have shown that the average DNA protein complex length is 50% of the length found at 0.04 or 0.15 M NaCl.

摘要

通过电子显微镜研究了大肠杆菌DNA解旋蛋白与单链DNA的协同结合。借助一个简单的统计力学模型对电子显微镜数据进行分析,得出在0.15M NaCl中协同结合常数的值为3.8 - 7.6×10¹⁰ l/mol。在高盐条件下的研究表明,DNA - 蛋白质复合物的平均长度是在0.04M或0.15M NaCl中所发现长度的50%。

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Studies on the cooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA.大肠杆菌DNA解旋蛋白与单链DNA协同结合的研究。
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