Transient protein interactions studied by NMR spectroscopy: The case of cytochrome C and adrenodoxin
Transient protein interactions studied by NMR spectroscopy: The case of cytochrome C and adrenodoxin
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DOI：
10.1021/bi0342968
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发表时间：
2003-06-17
期刊：
影响因子：
2.9
通讯作者：
Ubbink, M
中科院分区：
文献类型：
--
作者：
Worrall, JAR;Reinle, W;Ubbink, M
The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional heteronuclear NMR spectroscopy. Chemical shift perturbations and line broadening of amide resonances in the [N-15,H-1]HSQC spectrum for both N-15-labeled cytochrome c and adrenodoxin in the presence of the unlabeled partner protein indicate the formation of a transient complex, with a K-a of (4 +/- 1) x 10(4) M-1 and a lifetime of
