[NMR paper] Accurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
Accurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
Related ArticlesAccurate Identification of Unknown and Known Metabolic Mixture Components by Combining 3D NMR with Fourier Transform Ion Cyclotron Resonance Tandem Mass Spectrometry.
J Proteome Res. 2017 Oct 06;16(10):3774-3786
Authors: Wang C, He L, Li DW, Bruschweiler-Li L, Marshall AG, Brüschweiler R
Abstract
Metabolite identification in metabolomics samples is a key step that critically impacts downstream analysis. We recently introduced the SUMMIT NMR/mass spectrometry (MS) hybrid approach for the identification of the molecular structure of unknown metabolites based on the combination of NMR, MS, and combinatorial cheminformatics. Here, we demonstrate the feasibility of the approach for an untargeted analysis of both a model mixture and E. coli cell lysate based on 2D/3D NMR experiments in combination with Fourier transform ion cyclotron resonance MS and MS/MS data. For 19 of the 25 model metabolites, SUMMIT yielded complete structures that matched those in the mixture independent of database information. Of those, seven top-ranked structures matched those in the mixture, and four of those were further validated by positive ion MS/MS. For five metabolites, not part of the 19 metabolites, correct molecular structural motifs could be identified. For E. coli, SUMMIT MS/NMR identified 20 previously known metabolites with three or more 1H spins independent of database information. Moreover, for 15 unknown metabolites, molecular structural fragments were determined consistent with their spin systems and chemical shifts. By providing structural information for entire metabolites or molecular fragments, SUMMIT MS/NMR greatly assists the targeted or untargeted analysis of complex mixtures of unknown compounds.
Combining H/D Exchange Mass Spectrometry and ComputationalDocking To Derive the Structure of Protein–Protein Complexes
Combining H/D Exchange Mass Spectrometry and ComputationalDocking To Derive the Structure of Protein–Protein Complexes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00643/20171116/images/medium/bi-2017-00643w_0002.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00643
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11-20-2017 02:16 PM
Beyond the Paradigm: Combining Mass Spectrometry and Nuclear Magnetic Resonance for Metabolomics
Beyond the Paradigm: Combining Mass Spectrometry and Nuclear Magnetic Resonance for Metabolomics
Publication date: Available online 11 January 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Darrell D. Marshall, Robert Powers</br>
Metabolomics is undergoing tremendous growth and is being employed to solve a diversity of biological problems from environmental issues to the identification of biomarkers for human diseases. Nuclear magnetic resonance (NMR) and mass spectrometry (MS) are the analytical tools that are routinely, but...
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01-11-2017 01:31 PM
[NMR paper] Amyloid Hydrogen Bonding Polymorphism Evaluated by (15)N{(17)O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.
Amyloid Hydrogen Bonding Polymorphism Evaluated by (15)N{(17)O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Amyloid Hydrogen Bonding Polymorphism Evaluated by (15)N{(17)O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.
Biochemistry. 2016 Apr 12;55(14):2065-8
Authors: Wei J, Antzutkin ON, Filippov...
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08-31-2016 02:34 PM
Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High ResolutionFourier Transform Ion Cyclotron Resonance Mass Spectrometry
Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High ResolutionFourier Transform Ion Cyclotron Resonance Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01095/20160401/images/medium/bi-2015-01095d_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01095
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04-02-2016 09:29 AM
[NMR paper] An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
Protein Sci. 2015 May 26;
Authors: Nyon MP, Prentice T, Day J, Kirkpatrick J, Sivalingam GN, Levy G, Haq I, Irving JA, Lomas DA, Christodoulou J, Gooptu B, Thalassinos K
...
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05-27-2015 10:39 AM
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
Abstract
Native mass spectrometry (MS) methods permit the study of multiple protein species within solution equilibria, whilst ion mobility (IM)-MS can report on conformational behaviour of specific states. We used IM-MS to study a conformationally labile protein (?1-antitrypsin) that undergoes pathological polymerisation in the context of point mutations. The folded, native state of the Z variant remains...
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05-26-2015 08:09 PM
[NMR paper] Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Related Articles Identification of differential protein binding affinities in an atropisomeric pharmaceutical compound using non-covalent mass spectrometry, equilibrium dialysis and NMR.
Anal Chem. 2013 May 22;
Authors: Maple HJ, Garlish RA, Whitcombe I, Hold A, Prosser CE, Ford D, Mackenzie H, Crosby J, Porter J, Taylor RJ, Crump MP
Abstract
Atropisomerism of...
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05-24-2013 10:44 PM
[NMR paper] G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment
G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.
Related Articles G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.
Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9642-7
Authors: Atreya HS, Szyperski T
A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise...