Related ArticlesExpanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression Host Scott Ross was helpful in conducting the 1D TOCSY NMR experiments and Pratip Bhattachary is thanked for assistance in other NMR experiments. We are grateful to Yves Mechulam for a sample of plasmid pBSM547W305F and to Hieronim Jakubowski of UMDNJ-New Jersey Medical School, Newark, New Jersey, for plasmid pGG3. K.L.K. thanks the U.S. Department of Defense for a National Defense Science and Engineering Graduate Fellowship. This work was supported by grants from the Polymers and Genetics Programs of the National Science Foundation and from the U.S. Army Research Office.
Angew Chem Int Ed Engl. 2000 Jun 16;39(12):2148-2152
Authors: Kiick KL, van Hest JC , Tirrell DA
PMID: 10941044 [PubMed - as supplied by publisher]
Generative probabilistic models extend the scope of inferential structure determination
Generative probabilistic models extend the scope of inferential structure determination
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 6 September 2011</br>
Simon, Olsson , Wouter, Boomsma , Jes, Frellsen , Sandro, Bottaro , Tim, Harder , ...</br>
Conventional methods for protein structure determination from NMR data rely on the ad hoc combination of physical forcefields and experimental data, along with heuristic determination of free parameters such as weight of experimental data relative to a physical forcefield....
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09-06-2011 08:17 PM
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200189u/aop/images/medium/bi-2011-00189u_0010.gif
Biochemistry
DOI: 10.1021/bi200189u
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04-13-2011 01:25 PM
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
Biochemistry. 2011 Mar 25;
Authors: Paukstelis PJ, Chari N, Lambowitz AM, Hoffman DW
The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina fungi are bifunctional proteins that aminoacylate mitochondrial tRNATyr and are structure-stabilizing splicing cofactors for group I introns. Studies with the Neurospora...
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03-29-2011 07:04 PM
Suppression of phospholipid biosynthesis by cerulenin in the condensed Single-Protein-Production (cSPP) system
Suppression of phospholipid biosynthesis by cerulenin in the condensed Single-Protein-Production (cSPP) system
Abstract Using the single-protein-production (SPP) system, a protein of interest can be exclusively produced in high yield from its ACA-less gene in Escherichia coli expressing MazF, an ACA-specific mRNA interferase. It is thus feasible to study a membrane protein by solid-state NMR (SSNMR) directly in natural membrane fractions. In developing isotope-enrichment methods, we observed that 13C was also incorporated into phospholipids, generating spurious signals in SSNMR spectra....
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02-03-2011 06:45 AM
[NMR paper] Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Related Articles Biosynthesis and NMR analysis of a 73-residue domain of a Saccharomyces cerevisiae G protein-coupled receptor.
Biochemistry. 2005 Sep 6;44(35):11795-810
Authors: Estephan R, Englander J, Arshava B, Samples KL, Becker JM, Naider F
The yeast Saccharomyces cerevisiae alpha-factor pheromone receptor (Ste2p) was used as a model G protein-coupled receptor (GPCR). A 73-mer multidomain fragment of Ste2p (residues 267-339)...
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12-01-2010 06:56 PM
[NMR paper] Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Related Articles Probing a CMP-Kdn synthetase by 1H, 31P, and STD NMR spectroscopy.
Biochem Biophys Res Commun. 2005 Feb 11;327(2):565-70
Authors: Haselhorst T, Münster-Kühnel AK, Stolz A, Oschlies M, Tiralongo J, Kitajima K, Gerardy-Schahn R, von Itzstein M
CMP-Kdn synthetase catalyses the reaction of sialic acids (Sia) and cytidine-5'-triphosphate (CTP) to the corresponding activated sugar nucleotide CMP-Sia and pyrophosphate PP(i). STD NMR experiments of a recombinant...
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11-24-2010 11:14 PM
[NMR paper] Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid pr
Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
Related Articles Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein.
J Mol Biol. 2001 Feb 23;306(3):443-54
Authors: Tisné C, Roques BP, Dardel F
Reverse transcription of HIV-1 viral RNA uses human tRNA(Lys)3 as a primer. Recombinant tRNA(Lys)3 was previously overexpressed in Escherichia coli, 15N-labelled and purified for NMR studies. It was shown to be functional for priming of HIV-1 reverse transcription. Using...