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¹H nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus

Rösch, P. and Kalbitzer, Hans-Robert and Schmidt-Aderjan, U. and Hengstenberg, W. (1981) ¹H nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus. Biochemistry 20 (6), pp. 1599-1605.

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Abstract

¹H NMR studies of the phosphocarrier protein HPr and its three nitrotyrosyl derivatives revealed some structural features which may finally lead to an explanation of the mechanism of the phospho-transfer reaction. Titration studies on mononitrated, dinitrated, and trinitrated derivatives--i.e., derivatives with Tyr-56, Tyr-56 and Tyr-37, and Tyr-56, Tyr-37, and Tyr-6 modified--have been ...

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Item Type:Article
Date:1981
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
7225348PubMed ID
Classification:
NotationType
Bacterial ProteinsMESH
Carrier ProteinsMESH
Chemical PhenomenaMESH
ChemistryMESH
Hydrogen-Ion ConcentrationMESH
Magnetic Resonance SpectroscopyMESH
Nitro CompoundsMESH
Phosphoenolpyruvate Sugar Phosphotransferase SystemMESH
Tyrosine/analogs & derivativesMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:03 Sep 2010 12:39
Last Modified:03 Sep 2010 12:39
Item ID:16423
Owner Only: item control page
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