Related ArticlesApplication of Two-Dimensional NMR Spectroscopy to Metabotyping Laboratory Escherichia coli Strains.
Chem Biodivers. 2013 Oct;10(10):1816-1827
Authors: Chae YK, Kim SH, Nam YK
Abstract
NMR Spectroscopy has been established as a major tool for identification and quantification of metabolites in a living system. Since the metabolomics era began, one-dimensional NMR spectroscopy has been intensively employed due to its simplicity and quickness. However, it has suffered from an inevitable overlap of signals, thus leading to inaccuracy in identification and quantification of metabolites. Two-dimensional (2D) NMR has emerged as a viable alternative because it can offer higher accuracy in a reasonable amount of time. We employed (1) H,(13) C-HSQC to profile metabolites of six different laboratory E. coli strains. We identified 18 metabolites and observed clustering of six strains according to their metabolites. We compared the metabolites among the strains, and found that a) the strains specialized for protein production were segregated; b) XL1-Blue separated itself from others by accumulating amino acids such as alanine, aspartate, glutamate, methionine, proline, and lysine; c) the strains specialized for cloning purpose were spread out from one another; and d) the strains originating from B strain were characterized by succinate accumulation. This work shows that 2D-NMR can be applied to identify a strain from metabolite analysis, offering a possible alternative to genetic analysis to identify E. coli strains.
PMID: 24130025 [PubMed - as supplied by publisher]
[NMR paper] Tracing Metabolite Footsteps of Escherichia coli Along the Time Course of Recombinant Protein Expression by Two-Dimensional NMR Spectroscopy.
Tracing Metabolite Footsteps of Escherichia coli Along the Time Course of Recombinant Protein Expression by Two-Dimensional NMR Spectroscopy.
Related Articles Tracing Metabolite Footsteps of Escherichia coli Along the Time Course of Recombinant Protein Expression by Two-Dimensional NMR Spectroscopy.
Bull Korean Chem Soc. 2012 Dec 20;33(12):4041-4046
Authors: Chae YK, Kim SH, Ellinger JJ, Markley JL
Abstract
The recombinant expression of proteins has been the method of choice to meet the demands from proteomics and structural genomics...
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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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[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.
Related Articles Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
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] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] Escherichia coli diacylglycerol kinase: a case study in the application of solution N
Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Escherichia coli diacylglycerol kinase: a case study in the application of solution NMR methods to an integral membrane protein.
Biophys J. 1997 Jun;72(6):2688-701
Authors: Vinogradova O,...
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[NMR paper] Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli phosphatidylgl
Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli phosphatidylglycerophosphate synthase in micelles.
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 Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli phosphatidylglycerophosphate synthase in micelles.
Eur J Biochem. 1996 Oct 15;241(2):489-97
Authors: Morein S, Trouard TP, Hauksson JB, Rilfors L, Arvidson G, Lindblom G
Two 28-residue...
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[NMR paper] 19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate redu
19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Related Articles 19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Biochemistry. 1994 May 10;33(18):5502-9
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan...
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[NMR paper] 19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate redu
19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Related Articles 19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Biochemistry. 1994 May 10;33(18):5502-9
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan...