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  The phosphoenolpyruvate‐dependent phosphotransferase system of Staphylococcus aureus 3. 1H and 31P nuclear‐magnetic‐resonance studies on the phosphocarrier protein HPr; tyrosine titration and denaturation studies

Maurer, W., Rüterjans, H., Schrecker, O., Hengstenberg, W., Gassner, M. K., & Stehlik, D. (1977). The phosphoenolpyruvate‐dependent phosphotransferase system of Staphylococcus aureus 3. 1H and 31P nuclear‐magnetic‐resonance studies on the phosphocarrier protein HPr; tyrosine titration and denaturation studies. European Journal of Biochemistry, 75(1), 297-301. doi:10.1111/j.1432-1033.1977.tb11529.x.

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EurJBiochem_75_1977_297.pdf (Any fulltext), 392KB
 
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Maurer, Wolfgang, Author
Rüterjans, Heinz, Author
Schrecker, Otto1, Author           
Hengstenberg, Wolfgang1, Author           
Gassner, Martin K.1, Author           
Stehlik, Dietmar1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: The phosphocarrier protein HPr has been investigated by proton nuclear magnetic resonance (NMR) at 270 MHz in order to evaluate structural properties of the whole molecule and its active site. The titration behaviour of the three tyrosines of the HPr protein was analysed by monitoring the chemical shifts of the aromatic proton resonances of these residues as a function of pH. It was found that the HPr protein contains a lot of slowly exchanging NH backbone protons which suggested a relatively rigid secondary structure of the protein molecule itself although it contains no disulfide bridges. The HPr protein shows a sharp reversible denaturation behaviour at alkaline pH values. Between pH 10.8 and 11.1 two C‐2 proton resonance peaks for the single histidine residue could be observed together with abrupt changes in the aromatic and aliphatic absorption region of the HPr protein which are due to chemical exchange processes. The NMR spectrum of the HPr protein is only changed a little upon raising the temperature from 14°C to 70°C. At 76°C all resonances in the spectrum broaden and almost disappear. This process is irreversible.

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Language(s): eng - English
 Dates: 1976-07-152008-06-281977-05
 Publication Status: Published in print
 Pages: 5
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 Rev. Type: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 75 (1) Sequence Number: - Start / End Page: 297 - 301 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040