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  Identification of valine/leucine/isoleucine and threonine/alanine/glycine proton-spin systems of Escherichia coli adenylate kinase by selective deuteration and selective protonation

Bock-Möbius, I., Brune, M., Wittinghofer, A., Zimmermann, H., Lebermann, R., Dauvergne, M.-T., et al. (1991). Identification of valine/leucine/isoleucine and threonine/alanine/glycine proton-spin systems of Escherichia coli adenylate kinase by selective deuteration and selective protonation. Biochemical Journal, 273(2), 311-316. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/1991031.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AC91-A Version Permalink: http://hdl.handle.net/21.11116/0000-0000-7482-A
Genre: Journal Article

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BiochemJ_273_1991_311.pdf (Any fulltext), 543KB
 
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Bock-Möbius, Imke, Author
Brune, Martin, Author
Wittinghofer, Alfred1, Author              
Zimmermann, Herbert1, 2, 3, Author              
Lebermann, Reuben, Author
Dauvergne, Marie-Thérèsa, Author
Zimmermann, Sabine3, Author              
Brandmeier, Birgit, Author
Rösch, Paul1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Molecular Physics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497705              
3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Adenylate kinase from two types of Escherichia coli strains, a wild-type and a leucine-auxotrophic strain, was purified. On the one hand, growing the leucine-auxotrophic bacteria on a medium containing deuterated leucine yielded E. coli adenylate kinase with all leucine residues deuterated. On the other hand, by growing the wild-type bacteria on deuterated medium with phenylalanine, threonine and isoleucine present as protonated specimens, 80% randomly deuterated enzyme with protonated phenylalanine, threonine and isoleucine residues could be prepared. Use of these proteins enabled identification of the spin systems of these amino acid residues in the n.m.r. spectra of the protein.

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Language(s): eng - English
 Dates: 1991-01-151991-01-15
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Biochemical Journal
Source Genre: Journal
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Publ. Info: London : Published by Portland Press on behalf of the Biochemical Society.
Pages: - Volume / Issue: 273 (2) Sequence Number: - Start / End Page: 311 - 316 Identifier: ISSN: 0264-6021
CoNE: https://pure.mpg.de/cone/journals/resource/110992357308158