[NMR paper] 1H, 13C and 15*N NMR assignments of solubility tag protein Msyb of Escherichia coli.
1H, 13C and 15*N NMR assignments of solubility tag protein Msyb of Escherichia coli.
Related Articles 1H, 13C and 15*N NMR assignments of solubility tag protein Msyb of Escherichia coli.
Biomol NMR Assign. 2020 Jun 05;:
Authors: Yang Y, Ke Z, Wang Z, Li Y, Li Y, Wang Y, Liu B
Abstract
Biochemical and structural characterizations of a protein are the prerequisite for the further understanding of its biological role and potential applications. The expression of recombinant protein is almost unavoidable to produce the amount of the...
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06-08-2020 02:01 AM
The Stories Tryptophans Tell: Exploring Protein Dynamicsof Heptosyltransferase I from Escherichia coli
The Stories Tryptophans Tell: Exploring Protein Dynamicsof Heptosyltransferase I from Escherichia coli
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00850/20170130/images/medium/bi-2016-00850w_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00850
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01-31-2017 06:20 AM
[NMR paper] Strategies for Protein NMR in Escherichia coli.
Strategies for Protein NMR in Escherichia coli.
Related Articles Strategies for Protein NMR in Escherichia coli.
Biochemistry. 2014 Mar 5;
Authors: Xu G, Ye Y, Liu X, Cao S, Wu Q, Cheng K, Liu M, Pielak GJ, Li C
Abstract
In-cell NMR spectroscopy provides insight into protein conformation, dynamics and function at atomic resolution in living cells. Systematic evaluation of isotopic labeling strategies is necessary to observe the target protein in the sea of other molecules in the cell. Here, we investigate the detectability, sensitivity and...
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03-08-2014 06:52 AM
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
(1)H, (13)C and (15)N NMR assignments of the Escherichia coli Orf135 protein.
Biomol NMR Assign. 2011 May 7;
Authors: Kawasaki K, Yoneyama M, Murata-Kamiya N, Harashima H, Kojima C, Ito Y, Kamiya H, Mishima M
Escherichia coli Orf135 protein is thought to be an enzyme that efficiently hydrolyzes oxidatively damaged nucleotides such as 2-hydroxy-dATP, 8-hydroxy-dGTP and 5-hydroxy-CTP, in addition to 5-methyl-dCTP, dCTP and CTP, thus preventing mutations in cells caused by...
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05-10-2011 05:11 PM
[NMR paper] NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in so
NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Related Articles NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Protein Sci. 2005 Apr;14(4):1082-90
Authors: Wang G, Peterkofsky A, Keifer PA, Li X
The solution form of IIA(Ntr) from Escherichia coli and its interaction with its partner protein, NPr, were characterized by nuclear magnetic resonance (NMR)...
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11-24-2010 11:14 PM
[NMR paper] NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zin
NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Related Articles NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Proteins. 2002 Nov 1;49(2):289-93
Authors: Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA
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[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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11-18-2010 08:31 PM
[NMR paper] Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
Related Articles Proton 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...
Protein 19F NMR in Escherichia coli - ACS Publications
Linear Mode
