Proximity relationship between the active site of Escherichia coli RNA polymerase and rifampicin binding domain: a resonance energy-transfer study
- 25 August 1992
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 31 (33) , 7519-7526
- https://doi.org/10.1021/bi00148a012
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 26 references indexed in Scilit:
- Structural studies on the active site of Escherichia coli RNA polymerase. 2. Geometrical relationship of the interacting substratesBiochemistry, 1990
- Structural studies on the active site of Escherichia coli RNA polymerase. 1. Interaction of metals on the i and i + 1 sitesBiochemistry, 1990
- Selective substitution in vitro of an intrinsic zinc of Escherichia coli RNA polymerase with various divalent metalsBiochemistry, 1982
- Direct coordination of nucleotide with the intrinsic metal in Escherichia coli RNA polymerase. A nuclear magnetic resonance study with cobalt-substituted enzymeBiochemistry, 1982
- [17] Time-resolved fluorescence measurementsPublished by Elsevier ,1979
- Intramolecular energy transfer and molecular conformation.Proceedings of the National Academy of Sciences, 1976
- Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatographyBiochemistry, 1975
- Fluorescence Quantum Yield Measurements: Vitamin B 6 CompoundsScience, 1965
- BORAX TO BORANESAnalytical Chemistry, 1963
- Zwischenmolekulare Energiewanderung und FluoreszenzAnnalen der Physik, 1948