Two-dimensional proton NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments
- 18 November 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (23) , 7760-7769
- https://doi.org/10.1021/bi00371a071
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 10 references indexed in Scilit:
- Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate/sugar phosphotransferase systemBiochemistry, 1985
- Proton NMR studies of .lambda. cro repressor. 1. Selective optimization of two-dimensional relayed coherence transfer spectroscopyBiochemistry, 1985
- Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distancesJournal of Molecular Biology, 1984
- The primary structure of Salmonella typhimurium HPr, a phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system. A correction.Journal of Biological Chemistry, 1984
- Sugar transport by the bacterial phosphotransferase system. Primary structure and active site of a general phosphocarrier protein (HPr) from Salmonella typhimurium.Journal of Biological Chemistry, 1982
- HPr proteins of different microorganisms studied by proton-high-resolution nuclear magnetic resonance: similarities of structures and mechanismsBiochemistry, 1982
- Preliminary X-ray data for the HPr protein of the phosphoenolpyruvate: Sugar phosphotransferase system of Escherichia coliJournal of Molecular Biology, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some propertiesCanadian Journal of Biochemistry, 1980
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979