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Proton-nuclear magnetic resonance studies of the aromatic spin systems of Escherichia coli adenylate kinase

MPG-Autoren
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Reinstein,  Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Rösch,  Paul
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Bock, I., Reinstein, J., Brune, M., Wittinghofer, A., & Rösch, P. (1988). Proton-nuclear magnetic resonance studies of the aromatic spin systems of Escherichia coli adenylate kinase. Journal of Molecular Biology (London), 200(4), 745-748. doi:10.1016/0022-2836(88)90486-X.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-AE59-9
Zusammenfassung
Escherichia coli adenylate kinase has a very well resolved proton nuclear magnetic resonance spectrum in the region containing signals from aromatic amino acid side-chains. We found that the protein is structurally stable over a wide pH range and renatures spontaneously after acidic as well as basic denaturation. Only one out of the three histidyl imidazole rings titrates on changing the pH and has a pka value of 7.6. Two-dimensional nuclear magnetic resonance spectroscopy studies allowed use to identify most of the enzyme's aromatic spin systems, and by investigation of a mutant protein we were able to assign the aromatic part of the spin system of Tyr24 unambiguously.