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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 and Hengstenberg, W. and Rösch, P. and Muss, P. and Bernsmann, P. and Engelmann, R. and Dörschug, M. and Deutscher, J. (1982) HPr proteins of different microorganisms studied by hydrogen-1 high-resolution nuclear magnetic resonance: similarities of structures and mechanisms. Biochemistry 21 (12), pp. 2879-2885.

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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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Item Type:Article
Date:1982
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
6809041PubMed ID
Classification:
NotationType
Bacillus subtilis/metabolismMESH
Bacterial ProteinsMESH
Binding SitesMESH
Carrier Proteins/metabolismMESH
Enterococcus faecalis/metabolismMESH
Escherichia coli/metabolismMESH
EvolutionMESH
HistidineMESH
Hydrogen-Ion ConcentrationMESH
Lactococcus lactis/metabolismMESH
Magnetic Resonance SpectroscopyMESH
Phosphoenolpyruvate Sugar Phosphotransferase SystemMESH
Species SpecificityMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:02 Sep 2010 06:40
Last Modified:02 Sep 2010 06:40
Item ID:16429
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