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Disordered proteins:
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Default Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C

Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.

Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.

Biochemistry. 2003 Jun 17;42(23):7068-76

Authors: Worrall JA, Reinle W, Bernhardt R, 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 [(15)N,(1)H]HSQC spectrum for both (15)N-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
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