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HPr proteins of different microorganisms studied by hydrogen-1 high-resolution nuclear magnetic resonance: similarities of structures and mechanisms

Kalbitzer, Hans Robert ; Hengstenberg, W. ; Rösch, P. ; Muss, P. ; Bernsmann, P. ; Engelmann, R. ; Dörschug, M. ; Deutscher, J.



Abstract

The HPr proteins of Streptococcus lactis, Streptococcus faecalis, Bacillus subtilis, and Escherichia coli were studied by 1H NMR at 360 MHz. The "active-center" histidines of all HPr proteins are characterized by a low pK value between 5.6 and 6.1 and similar spectral parameters. Phosphorylation of the histidyl residues leads to an increase of the pK value of 2-3 units and spectral changes ...

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