Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 2. Leucine resonance assignments by long-range coherence transfer.
Sequence-specific assignments of the NH, C alpha H, and C beta H resonances in the NMR spectrum of the histidine-containing protein (HPr) from Escherichia coli are complete [Klevit, R. E., Drobny, G. P., & Waygood, E. B. (1986) Biochemistry (first paper of three in this issue)]. In addition, the C gamma H3 resonances of valyl, threonyl, and isoleucyl residues have been assigned by two-dimensional relayed coherence transfer (RELAY) experiments. In order to rigorously assign the resonances from longer side chains such as leucines, long-range transfer experiments have been applied to HPr. Coherence transfers via isotropic mixing within large spin systems were accomplished by multiple pulse trains applied during the mixing time of a two-dimensional experiment.
D001426:Bacterial Proteins; D004926:Escherichia coli / Q000201:enzymology*; D006859:Hydrogen; D007700:Kinetics; D007930:Leucine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*
D001426:Bacterial Proteins; D006859:Hydrogen; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; D007930:Leucine