Publication year: 2010 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 1 July 2010
Eugene C., Lin , Chin H., Wu , Yuan, Yang , Christopher V., Grant , Stanley J., Opella
By incorporating homonuclear decoupling on both the 1H and 13C channels it is feasible to obtain high-resolution two-dimensional separated local field spectra of peptides and proteins that are 100% labeled with 13C. Dual-PISEMO (Polarization Inversion Spin Exchange Modulated Observation) can be performed as a conventional two-dimensional experiment, or with windowed detection as a one-dimensional experiment that offers flexibility as a building block for Shiftless and other multidimensional triple-resonance experiments with the inclusion of 15N irradiation. The triple-resonance MAGC probe used to perform these experiments at 500 MHz is described.
[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Related Articles Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
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[NMR paper] Auto-induction medium for the production of [U-15N]- and [U-13C, U-15N]-labeled prote
Auto-induction medium for the production of - and -labeled proteins for NMR screening and structure determination.
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Protein Expr Purif. 2005 Apr;40(2):268-78
Authors: Tyler RC, Sreenath HK, Singh S, Aceti DJ, Bingman CA, Markley JL, Fox BG
Protocols have been developed and applied for the high-throughput production of - or -labeled proteins using the conditional methionine auxotroph Escherichia coli B834. The...
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[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
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Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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[NMR paper] NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Prote
NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Protein
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Protein
J Magn Reson. 1997 May;126(1):48-57
Authors: Allard P, Härd T
The predominant relaxation mechanisms for backbone carbonyl carbon (13 C') relaxation in a 13 C, 15 N-doubly enriched sample of the thermostable Sso7d protein have been investigated....
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[NMR paper] Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide
Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide for NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide for NMR studies.
Nucleic Acids Res. 1997 Apr 1;25(7):1390-6
Authors: Nikonowicz EP,...
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08-22-2010 03:31 PM
[NMR paper] NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Prote
NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Protein
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Protein
J Magn Reson. 1997 May;126(1):48-57
Authors: Allard P, Härd T
The predominant relaxation mechanisms for backbone carbonyl carbon (13 C') relaxation in a 13 C, 15 N-doubly enriched sample of the thermostable Sso7d protein have been investigated....
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08-22-2010 03:03 PM
[NMR paper] Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide
Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide for NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Preparation and characterization of a uniformly 2 H/ 15 N-labeled RNA oligonucleotide for NMR studies.
Nucleic Acids Res. 1997 Apr 1;25(7):1390-6
Authors: Nikonowicz EP,...
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Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Patrik Lundström, D. Flemming Hansen and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 42(1); pp 35 - 47
Abstract: Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy has emerged as a powerful method for quantifying chemical shifts of excited protein states. For many applications of the technique that involve the measurement of relaxation rates of carbon...
1H-13C Separated Local Field Spectroscopy of Uniformly 13C Labeled Peptides and Prote
Linear Mode
