Netropsin specifically recognizes one of the two conformationally equivalent strands of poly(dA).poly(dT). One dimensional NMR study at 500 MHz involving NOE transfer between netropsin and DNA protons.
Netropsin specifically recognizes one of the two conformationally equivalent strands of poly(dA).poly(dT). One dimensional NMR study at 500 MHz involving NOE transfer between netropsin and DNA protons.
复制标题
Netropsin 特异性识别聚 (dA).聚 (dT) 的两条构象等效链之一。
DOI:
10.1080/07391102.1985.10507625
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发表时间:
1985
影响因子:
4.4
通讯作者:
Sarma,RH
中科院分区:
文献类型:
--
作者:
Sarma,MH;Gupta,G;Sarma,RH
Recent observations that the heteronomous structural model for poly(dA)·poly(dT) is not found in solution and that in this DNA, the two strands are conformationally equivalent(J. Biomole. Str. Dyns. 2, 1057 (1985)), has added a new dimension to the structural dynamics of DNA-netropsin complex. Does the antibiotic somehow distinguish between the two strands and specifically interact with only one of the conformationally equivalent strands?Model-building studies suggest that netropsin can either bind to the dA-strand in the minor groove such that H-bonds are formed between the imino protons N4-H, N6-H, N8-H of netropsin and N3 atoms of A or can bind to the dT-strand in the minor groove and form H-bonds between the imino-protons N4-H, N6-H, N8-H of netropsin and O2 atoms of T. If netropsin binds to the dA-strand, AH2 atoms of poly(dA)-poly(dT) would be in closer proximity to the imino protrons N4-H, N6-H, N8-H and pyrrole ring protons C5-H, Cll-H of netropsin than they would be, if netropsin binds to the dT-strand. In order to distinguish these possibilities experiments were conducted which involved NOE energy transfer between netropsin and DNA protons in the drug-DNA complex. Difference NOE spectra of netropsin·poly(dA)-poly(dT) complex in which AH2 was irradiated indicate that dominant NOEs were observed at the imino and pyrrole ring protons of netropsin. When the netropsin pyrrole ring protons were irradiated, the magnetization transfer was at AH2 of DNA. These observations suggest that netropsin binds to the dA-strand of poly(dA)-poly(dT) even though dA/dT strands are conformationally equivalent.
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影响因子:
4.4
作者:
J. Rubin;M. Sundaralingam
通讯作者:
M. Sundaralingam
DOI:
--
发表时间:
1979
期刊:
European Journal of Biochemistry
影响因子:
--
作者:
D. Patel
通讯作者:
D. Patel
影响因子:
4.4
作者:
Gupta,G;Sarma,MH;Sarma,RH
通讯作者:
Sarma,RH
影响因子:
4.4
作者:
K. Zakrzewska;B. Pullman
通讯作者:
B. Pullman
DOI:
--
发表时间:
1982
影响因子:
11.1
作者:
D. Patel
通讯作者:
D. Patel