When planning a fluorine labeling strategy for 19F solid state NMR (ssNMR) studies of the structure and/or mobility of fluorine labeled compounds in situ in an oriented biological system, it is important to characterize the NMR properties of the label. This manuscript focuses on the characterization of a selection of aromatic fluorine compounds in dimyristoylphosphatidylcholine bilayers using 19F ssNMR from the standpoint of determiningÂ*the optimum arrangement of fluorine nuclei on a pendant aromatic ring before incorporation into more complex biological systems.
[NMR paper] Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
Related Articles Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
J Biomol NMR. 2018 Jun 12;:
Authors: Wiegand T, Cadalbert R, von Schroetter C, Allain FH, Meier BH
Abstract
Segmental isotope labelling enables the NMR study of an individual domain within a multidomain protein, but still in the context of the entire full-length protein....
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06-28-2018 02:38 PM
Segmental isotope labelling and solid-state NMR of a 12â??Ã?â??59Â*kDa motor protein: identification of structural variability
Segmental isotope labelling and solid-state NMR of a 12â??Ã?â??59Â*kDa motor protein: identification of structural variability
Abstract
Segmental isotope labelling enables the NMR study of an individual domain within a multidomain protein, but still in the context of the entire full-length protein. Compared to the fully labelled protein, spectral overlap can be greatly reduced. We here describe segmental labelling of the (double-) hexameric DnaB helicase from Helicobacter pylori using a ligation approach. Solid-state spectra demonstrate that the...
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06-12-2018 08:40 AM
[NMR paper] Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Chem Commun (Camb). 2016 Jul 7;
Authors: Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda P
Abstract
Solid-state NMR spectroscopy allows the characterization of the structure, interactions and dynamics of insoluble...
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07-08-2016 10:02 PM
[NMR paper] Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.
Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.
Related Articles Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.
J Biomol NMR. 2016 Apr 27;
Authors: Liu J, Liu C, Fan Y, Munro RA, Ladizhansky V, Brown LS, Wang S
Abstract
We demonstrate a novel sparse (13)C labelling approach for methylotrophic yeast P. pastoris expression system, towards solid-state NMR studies of eukaryotic membrane proteins....
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04-29-2016 06:31 PM
Sparse 13 C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins
Sparse 13 C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins
Abstract
We demonstrate a novel sparse 13C labelling approach for methylotrophic yeast P. pastoris expression system, towards solid-state NMR studies of eukaryotic membrane proteins. The labelling scheme was achieved by co-utilizing natural abundance methanol and specifically 13C labelled glycerol as carbon sources in the expression medium. This strategy improves the spectral resolution by 1.5 fold, displays site-specific labelling...
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04-28-2016 02:15 PM
[NMR paper] An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.
An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.
Related Articles An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in (1) H-Detected Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Nov 11;
Authors: Mance D, Sinnige T, Kaplan M, Narasimhan S, Daniëls M, Houben K, Baldus M, Weingarth M
Abstract
(1) H-detection can greatly improve spectral sensitivity in biological solid-state NMR (ssNMR), thus allowing the study of larger...
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11-12-2015 11:28 PM
Optimizing sample preparation methods for dynamic nuclear polarization solid-state NMR of synthetic polymers
From The DNP-NMR Blog:
Optimizing sample preparation methods for dynamic nuclear polarization solid-state NMR of synthetic polymers
Le, D., et al., Optimizing sample preparation methods for dynamic nuclear polarization solid-state NMR of synthetic polymers. Macromolecules, 2014: p. 140613123939001.
http://pubs.acs.org/doi/abs/10.1021/ma500788n
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06-18-2014 06:09 PM
[NMR paper] Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Related Articles Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Biophys J. 2005 Oct;89(4):2792-805
Authors: Rainey JK, Sykes BD
Sample orientation relative to the static magnetic field of an NMR spectrometer allows study of membrane proteins in the lipid bilayer setting. The straightforward preparation and handling of extremely thin mica substrates with consistent surface properties has prompted us to examine oriented phospholipid...
Optimizing fluorine labelling for 19 F solid-state NMR in oriented biological systems
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