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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AE59-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0002-6A58-5
Genre: Journal Article

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JMolBiol_200_1988_745.pdf (Any fulltext), 374KB
 
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 Creators:
Bock, Imke, Author
Reinstein, Jochen1, Author           
Brune, Martin, Author
Wittinghofer, Alfred2, Author           
Rösch, Paul2, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 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.

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Language(s): eng - English
 Dates: 1987-09-011988-04-20
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0022-2836(88)90486-X
URI: https://www.ncbi.nlm.nih.gov/pubmed/2842509
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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 200 (4) Sequence Number: - Start / End Page: 745 - 748 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042