ASPECTS OF SPECIFIC PROTEIN-DNA INTERACTION - MULTIMODE BINDING OF THE OLIGOPEPTIDE ANTIBIOTIC NETROPSIN TO (A.T)-RICH DNA SEGMENTS

被引:51
作者
REINERT, KE
STUTTER, E
SCHWEISS, H
机构
[1] Academy of Sciences of GDR, Central Institute of Microbiology and Experimental Therapy, Department of Biophysical Chemistry
关键词
D O I
10.1093/nar/7.5.1375
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
By means of titration viscometry a number of distinct modes could be resolved for the interaction between the antibiotic netropsln and DNA species of 50, 58, and 69 mole % (A+T) below r = 0.04 netropsln molecules bound per DNA phosphate group. The number of corresponding binding sites increases with a high power of the (A+T) gontent. The apparent association constants are very high (>106 M-1 some perhaps≫106 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. © 1979 Information Retrieval Limited.
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页码:1375 / 1392
页数:18
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