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NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase.
The bacterial toxin colicin E9 is secreted by producing Escherichia coli cells with its 9.5 kDa inhibitor protein Im9 bound tightly to its 14.5 kDa C-terminal DNase domain. Double- and triple-resonance NMR spectra of the 24 kDa complex of uniformly 13C and 15N labeled Im9 bound to the unlabeled DNas...
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| Hlavní autoři: | , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2000
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144694/ https://ncbi.nlm.nih.gov/pubmed/11045617 |
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