Related ArticlesFrontispiece: Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Chemistry. 2015 Jun 8;21(24)
Authors: Ye Y, Liu X, Chen Y, Xu G, Wu Q, Zhang Z, Yao C, Liu M, Li C
Abstract
NMR Spectroscopy In their Communication on page 8686 ff., C. Li et al., demonstrate that (19) F labeling is a good first choice for studying globular and disordered proteins in Xenopus oocytes, especially compared with conventional (15) N- or (13) C-methyl enrichment. By using (19) F labeling, they found that, unlike E. coli cells, the viscosity in oocytes is only about 1.2 times that of water and that inhomogeneous broadening contributes 60-70 % to the line width. The labeling strategies and resonance broadening mechanisms in Xenopus oocytes were explored with the goal of expanding the application of this cell type.
[NMR paper] Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Chemistry. 2015 May 12;
Authors: Ye Y, Liu X, Chen Y, Xu G, Wu Q, Zhang Z, Yao C, Liu M, Li C
Abstract
We used Xenopus laevis oocytes, a paradigm for a variety of biological studies, as a eukaryotic model system for in-cell protein NMR spectroscopy. The small globular protein GB1 was one of the first studied in...
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05-13-2015 02:01 PM
[NMR paper] Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
PLoS One. 2015;10(4):e0122714
Authors: Wang S, Parthasarathy S, Nishiyama Y, Endo Y, Nemoto T, Yamauchi K, Asakura T,...
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[NMR paper] Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Mar 5;
Authors: Ye Y, Liu X, Xu G, Liu M, Li C
Abstract
The...
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[NMR paper] Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Angew Chem Int Ed Engl. 2014 Apr 22;53(17)
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J,...
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04-23-2014 06:31 PM
[NMR paper] NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
Related Articles NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
J Biomol NMR. 2005 Mar;31(3):260
Authors: Pérez DR, Wüthrich K
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[NMR paper] Differential isotype labeling strategy for determining the structure of myristoylated
Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy.
Related Articles Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy.
J Biomol NMR. 1998 Feb;11(2):135-52
Authors: Tanaka T, Ames JB, Kainosho M, Stryer L, Ikura M
The three-dimensional solution structure of recombinant bovine myristoylated recoverin in the Ca(2+)-free state has been refined using an array of isotope-assisted multidimensional heteronuclear NMR...
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11-17-2010 11:06 PM
A simple strategy for 13C,1H labeling at the Ile-γ2 methyl position in highly deuter
A simple strategy for 13C,1H labeling at the Ile-γ2 methyl position in highly deuterated proteins
Abstract A straightforward approach for the production of highly deuterated proteins labeled with 13C and 1H at Ile-γ2 methyl positions is described. The utility of the methodology is illustrated with an application involving the half proteasome (360 kDa). High quality 2D Ile 13Cγ2,1Hγ2 HMQC data sets, exploiting the methyl-TROSY principle, are recorded with excellent sensitivity and resolution, that compare favorably with Ile 13Cδ1,1Hδ1 spectra. This labeling scheme adds to a growing...
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10-20-2010 06:50 AM
[NMR paper] Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of
Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
Protein Expr Purif. 1997 Oct;11(1):79-85
Authors: Okar DA, Felicia ND, Gui L, Lange AJ
Methods for the efficient use of the 13C-labeled nutrients,...
Frontispiece: Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
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