Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Monitoring Mechanistic Details in the Synthesis of Pyrimidines via Real-Time, Ultrafast Multidimensional NMR Spectroscopy
Zulay D. Pardo, Gregory L. Olsen, Mari?a Encarnacio?n Ferna?ndez-Valle, Lucio Frydman, Roberto Marti?nez-A?lvarez and Antonio Herrera
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210154g/aop/images/medium/ja-2011-10154g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210154g
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01-28-2012 05:27 AM
Biomass production of site selective 13C/15N nucleotides using wild type and a transketolase E. coli mutant for labeling RNA for high resolution NMR
Biomass production of site selective 13C/15N nucleotides using wild type and a transketolase E. coli mutant for labeling RNA for high resolution NMR
Abstract Characterization of the structure and dynamics of nucleic acids by NMR benefits significantly from position specifically labeled nucleotides. Here an E. coli strain deficient in the transketolase gene (tktA) and grown on glucose that is labeled at different carbon sites is shown to facilitate cost-effective and large scale production of useful nucleotides. These nucleotides are site specifically labeled in C1â?² and C5â?² with...
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11-30-2011 10:45 PM
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field
Abstract Magic-angle spinning (MAS) solid-state NMR (SSNMR) spectroscopy of uniformly-13C,15N labeled protein samples provides insight into atomic-resolution chemistry and structure. Data collection efficiency has advanced remarkably in the last decade; however, the study of larger proteins is still challenged by relatively low resolution in comparison to solution NMR. In this study, we present a systematic analysis of SSNMR protein spectra acquired at 11.7, 17.6 and 21.1 Tesla (1H frequencies of...
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01-09-2011 12:46 PM
[NMR paper] Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp
Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
Related Articles Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
J Am Chem Soc. 2004 Mar 24;126(11):3390-1
Authors: Harper SM, Neil LC, Day IJ, Hore PJ, Gardner KH
Phototropins are light-activated kinases from plants that utilize light-oxygen-voltage (LOV) domains as blue light photosensors. Illumination of these domains leads to the formation of a covalent linkage between the protein and an...
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11-24-2010 09:25 PM
[NMR paper] Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation s
Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy.
Related Articles Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy.
Biophys J. 2004 Mar;86(3):1713-25
Authors: Teng CL, Bryant RG
Paramagnetic contributions to nuclear magnetic spin-lattice relaxation rate constant induced by freely diffusing molecular oxygen measured at hundreds of different protein proton sites provide a direct means for characterizing the exploration of the protein by oxygen. This...
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11-24-2010 09:25 PM
[NMR paper] High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspa
High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Related Articles High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Eur Biophys J. 1990;18(1):17-24
Authors: Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D
Three mutant strains of Halobacterium sp. GRB with the site of mutation in the bacterioopsin gene (PM 326:...
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08-21-2010 10:48 PM
Site-specific labeling of nucleotides for making RNA for high resolution NMR studies
Abstract Escherichia coli (E. coli) is a versatile organism for making nucleotides labeled with stable isotopes (13C, 15N, and/or 2H) for structural and molecular dynamics characterizations. Growth of a mutant E. coli strain deficient in the pentose phosphate pathway enzyme glucose-6-phosphate dehydrogenase (K10-1516) on 2-13C-glycerol and 15N-ammonium sulfate in Studier minimal medium enables labeling at sites useful for NMR spectroscopy. However, 13C-sodium formate combined with 13C-2-glycerol in the growth media adds labels to new positions. In the absence of labeled formate, both C5 and...
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08-14-2010 04:19 AM
Monitoring H-D exchange on second time scale with Frydman NMR spectroscopy
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Real-Time Monitoring of Chemical Transformations by Ultrafast 2D NMR Spectroscopy
Maayan Gal, Mor Mishkovsky, and Lucio Frydman
J. Am. Chem. Soc.; 2006; 128(3) pp 951 - 956;
Abstract:
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Linear Mode
