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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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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|Institutions:||Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer|
|Dewey Decimal Classification:||500 Science > 570 Life sciences|
|Created at the University of Regensburg:||Unknown|
|Deposited on:||02 Sep 2010 06:40|
|Last modified:||02 Sep 2010 06:40|