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

Bock, Imke; Reinstein, Jochen; Brune, Martin; Wittinghofer, Alfred; Rösch, Paul

doi:10.1016/0022-2836(88)90486-X

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

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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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http://www.sciencedirect.com/science/article/pii/002228368890486X/pdf?md5=c6640d86b30fe07c637e053c7f839bb9&pid=1-s2.0-002228368890486X-main.pdf
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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-AE59-9

Abstract

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.