Related ArticlesProton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
Biol Pharm Bull. 1993 May;16(5):437-43
Authors: Shindo H, Kurumizaka H, Furubayashi A, Sakuma C, Matsumoto U, Yanagida A, Goshima N, Kano Y, Imamoto F
It was confirmed that the flexible arm region of HU alpha forms an antiparallel beta-sheet and that all of the residues of phenylalanines, together with some of leucines and/or valines, form a hydrophobic core within the dimer of HU alpha. HU alpha protein alone is thermally labile and melts at 38 degrees C, but it becomes remarkably stabilized and melts at 59 degrees C in the presence of DNA. Several resonances from both HU alpha and DNA perturbed by their complex formation, notably those of His C-2 and C-4 protons, downfield shifted C alpha protons in the antiparallel beta-sheet, as well as Arg C delta and Lys C epsilon protons. The results indicated that a beta-sheet region of HU alpha binds to DNA, and also showed that rapid equilibrium occurs on the NMR time scale between bound and unbound states of HU alpha. A few intermolecular nuclear Overhauser effects (NOEs) were also observed between the protein and H1' protons of DNA in the complex, suggesting that HU alpha binds primarily to the minor groove of DNA.
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
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Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
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[NMR paper] Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
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Biochemistry. 2005 Sep 6;44(35):11786-94
Authors: Wilkens S, Borchardt D, Weber J, Senior AE
A critical point of interaction between F(1) and F(0) in the bacterial F(1)F(0)-ATP synthase is formed by the alpha and delta subunits. Previous work has...
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[NMR paper] 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesi
19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues.
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Protein Eng. 2002 Nov;15(11):855-9
Authors: Salopek-Sondi B, Luck LA
The Escherichia coli L-leucine receptor is an aqueous protein and the first component in the distinct transport pathway for hydrophobic amino acids. L-leucine binding...
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[NMR paper] Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit
Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands.
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Biochemistry. 1993 Aug 31;32(34):8782-91
Authors: Kaufman J, Siegel LM, Spicer LD
The heme protein subunit of sulfite reductase (SiR-HP; M(r) 64,000) from Escherichia coli as isolated contains the isobacteriochlorin siroheme exchange-coupled to a cluster in the 2+ oxidation state. SiR-HP in the presence of a suitable...
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[NMR paper] Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.
Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.
Related Articles Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.
Biochemistry. 1993 Mar 23;32(11):2853-67
Authors: Kaufman J, Spicer LD, Siegel LM
The isolated hemeprotein subunit of sulfite reductase (SiR-HP) from Escherichia coli consists of a high spin ferric isobacteriochlorin (siroheme) coupled to a diamagnetic 2+ cluster. When supplied with an artificial electron donor, such as methyl viologen cation radical, SiR-HP...
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[NMR paper] Proton-transfer effects in the active-site region of Escherichia coli thioredoxin usi
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
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Biochemistry. 1991 Apr 30;30(17):4262-8
Authors: Dyson HJ, Tennant LL, Holmgren A
A series of two-dimensional (2D) correlated 1H NMR spectra of reduced and oxidized Escherichia coli thioredoxin have been used to probe the effects of pH in the vicinity of the active site, -Cys32-Gly-Pro-Cys35-, using the...
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
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Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
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[NMR paper] 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containin
1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Related Articles 1H NMR study of the interaction of ATP with Escherichia coli RNA polymerase containing in vivo-incorporated Co(II).
Arch Biochem Biophys. 1991 Dec;291(2):307-10
Authors: Panth H, Brenner MC, Wu FY
The DNA-dependent RNA polymerase containing two intrinsic cobalt ions (Co2-RPase) instead of the naturally occurring zinc was purified from Escherichia coli cells grown in zinc-depleted, cobalt-enriched media....
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
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