[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
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Chembiochem. 2011 Mar 29;
Authors: Crowley PB, Chow E, Papkovskaia T
Protein science is shifting towards experiments performed under native or native-like conditions. In-cell NMR spectroscopy for instance has the potential to reveal protein structure and dynamics inside cells. However, not all proteins can be studied by this technique. (15) N-labelled...
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03-31-2011 06:24 PM
[NMR paper] Solution-state NMR investigation of DNA binding interactions in Escherichia coli form
Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
Related Articles Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
DNA Repair (Amst). 2005 Mar 2;4(3):327-39
Authors: Buchko GW, McAteer K, Wallace SS, Kennedy MA
Formamidopyrimidine-DNA glycosylase (Fpg) is a base excision repair (BER) protein...
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11-24-2010 11:14 PM
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...
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11-24-2010 11:14 PM
[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] Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 m
Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Related Articles Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Biochemistry. 1995 Oct 10;34(40):13183-9
Authors: Schmitt TH, Zheng Z, Jardetzky O
Binding of L-tryptophan to Escherichia coli trp repressor wild type (WT) and AV77 mutant was studied by 1H NMR spectroscopy. Ligand binding to the proteins resulted in changes in line widths and chemical shifts of ligand resonances, but...
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08-22-2010 03:50 AM
[NMR paper] The interactions of Escherichia coli trp repressor with tryptophan and with an operat
The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotide. NMR studies using selectively 15N-labelled protein.
Eur J Biochem. 1994 Oct 15;225(2):601-8
Authors: Ramesh V, Frederick RO, Syed SE,...
Substrate–Protein Interactions of Type II NADH:QuinoneOxidoreductase from Escherichia coli
Linear Mode
