期刊论文详细信息
FEBS Letters
31P NMR investigation of the backbone conformation and dynamics of the hexamer duplex d(5′‐GCATGC)2 in its complex with the antibiotic nogalamycin
Lane, Andrew N.2  Searle, Mark S.1 
[1] Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK;Laboratory of Molecular Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
关键词: 31P NMR relaxation;    (Nogalamycin)2/d(GCATGC)2;    Chemical shift anisotropy;    Correlation time;    1H−31P coupling;   
DOI  :  10.1016/0014-5793(92)80558-X
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Heteronuclear chemical shift correlation experiments confirm that the two down-field shifted 31P resonances in the spectrum of the (nogalamycin)2-d(GCATGC)2 complex correspond to the phosphodiesters CpA and TpG at the intercalation sites. 31P relaxation measurements (R1, R2 and {1H}-31P NOE) at 4.7 and 9.4 T permit the correlation time of each phosphate to be determined together with their chemical shift anisotropies. Significant differences in deoxyribose H3′−31P coupling constants and chemical shift anisotropy contributions are observed, consistent with an asymmetric DNA backbone conformation for the phosphate groups at the intercalation sites. Large amplitude internal motions of the phosphates do not appear to contribute significantly to relaxation.

【 授权许可】

Unknown   

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