Two-dimensional proton NMR studies of histidine-containing protein from Escherichia coli. 2. Leucine resonance assignments by long-range coherence transfer
- 18 November 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (23), 7770-7773
- https://doi.org/10.1021/bi00371a072
Abstract
Sequence-specific assignments of the NH, C.alpha.H, and C.beta.H resonances in the NMR spectrum of the histidne-containing protein (HPr) from Escherichia coli are complete [Klevit, R. E., Drobny, G. P., and Waygood, E. B. (1986) Biochemistry]. 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.This publication has 3 references indexed in Scilit:
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- An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solutionJournal of Molecular Biology, 1985
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