[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
[NMR paper] Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Related Articles Inverse Temperature Transition of Elastin Like Motifs in Major Ampullate Dragline Silk: MD Simulations of Short Peptides and NMR Studies of Water Dynamics.
Soft Matter. 2014 Feb 7;10(5):773-785
Authors: Ukpebor OT, Shah A, Bazov E, Boutis GS
Abstract
Using deuterium 2D T1-T2 Inverse Laplace Transform (ILT) NMR we have investigated the distribution, population, and...
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02-11-2014 09:58 PM
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Abstract Segmental isotopic labeling is a powerful labeling tool to facilitate NMR studies of larger proteins by not only alleviating the signal overlap problem but also retaining features of uniform isotopic labeling. Although two approaches, expressed protein ligation (EPL) and protein trans-splicing (PTS), have been mainly used for segmental isotopic labeling, there has been no single example in which both approaches have been...
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07-02-2012 06:18 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...