Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00995/20151215/images/medium/bi-2015-00995k_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00995
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nmrlearner
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12-16-2015 08:50 AM
[NMR paper] Mucoadhesivity and release properties of quaternary ammonium-chitosan conjugates and their nanoparticulate supramolecular aggregates: an NMR investigation.
Mucoadhesivity and release properties of quaternary ammonium-chitosan conjugates and their nanoparticulate supramolecular aggregates: an NMR investigation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mucoadhesivity and release properties of quaternary ammonium-chitosan conjugates and their nanoparticulate supramolecular aggregates: an NMR investigation.
Int J Pharm. 2014 Jan 30;461(1-2):489-94
Authors: Uccello-Barretta G, Balzano F, Aiello F, Senatore A,...
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10-01-2015 11:23 AM
[NMR paper] Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Biochim Biophys Acta. 2013 Jul 2;
Authors: Gautier A
Abstract
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical...
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07-09-2013 02:47 PM
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Publication date: Available online 2 July 2013
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics</br>
Author(s): Antoine Gautier</br>
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical reactions and mediate protein–protein interactions. Indeed, the...
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07-02-2013 09:44 AM
[NMR paper] NMR studies of a new family of DNA binding proteins: the THAP proteins.
NMR studies of a new family of DNA binding proteins: the THAP proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR studies of a new family of DNA binding proteins: the THAP proteins.
J Biomol NMR. 2013 Jan 11;
Authors: Gervais V, Campagne S, Durand J, Muller I, Milon A
Abstract
The THAP (THanatos-Associated Protein) domain is an evolutionary conserved C2CH zinc-coordinating domain shared with a large family of cellular factors (THAP proteins)....
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02-03-2013 10:22 AM
[Question from NMRWiki Q&A forum] 13C quaternary centers in amino acids
13C quaternary centers in amino acids
I've got a sample of about 5mg of an amino acid that is the final product of a a synthesis. Due to the long relaxation time that the carboxylic and the alpha C we only got a 200 varian Mercury instrument and we're unable to obtain those signals. I was wondering if an APT is better than DEPT, because we're only interested in this signals and i've heard the overall pulse sequence is shorter than the DEPT, increasing the number of scans in the same period of time.
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09-01-2011 07:20 AM
Engineering [Ln(DPA)3]3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Engineering 3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Abstract Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the protein via disulfide bonds, requiring proteins with single cysteine residues for covalent attachment. Here we present a straightforward strategy to tag proteins site-specifically with paramagnetic lanthanides without a tether and...
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07-26-2011 11:11 AM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
Quaternary Structure of Fur Proteins, a New Subfamily of Tetrameric Proteins
Linear Mode
