[NMR paper] Erratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Erratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Related ArticlesErratum to: Protein-protein interaction analysis in crude bacterial lysates using combinational method of (19)F site-specific incorporation and (19)F NMR.
Protein Cell. 2017 Mar 10;:
Authors: Li D, Zhang Y, He Y, Zhang C, Wang J, Xiong Y, Zhang L, Liu Y, Shi P, Tian C
PMID: 28284007 [PubMed - as supplied by publisher]
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Abstract
Nuclear magnetic resonance spectroscopy studies of ever larger systems have benefited from many different forms of isotope labeling, in particular, site specific isotopic labeling. Site specific 13C labeling of methyl groups has become an established means of probing systems not amenable to traditional methodology. However useful, methyl reporter sites can be limited in number and/or...
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NMR-BasedDetermination of the 3D Structure of theLigand–Protein Interaction Site without Protein Resonance Assignment
NMR-BasedDetermination of the 3D Structure of theLigand–Protein Interaction Site without Protein Resonance Assignment
Julien Orts, Marielle Aulikki Wa?lti, May Marsh, Laura Vera, Alvar D. Gossert, Peter Gu?ntert and Roland Riek
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b12391/20160323/images/medium/ja-2015-12391s_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b12391
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/np60JwjsRiM
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03-24-2016 04:18 AM
[NMR paper] NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment.
J Am Chem Soc. 2016 Mar 4;
Authors: Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, Riek R
Abstract
Molecular replacement in X-ray crystallography is the prime method for establishing structure-activity relationships of pharmaceutically relevant molecules. Such an approach is not...
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03-05-2016 11:21 AM
Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation
Persistent Activation of cGMP-Dependent Protein Kinaseby a Nitrated Cyclic Nucleotide via Site Specific Protein S-Guanylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00774/20160129/images/medium/bi-2015-00774n_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00774
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http://feeds.feedburner.com/~r/acs/bichaw/~4/KLjU9u3Nnwk
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01-30-2016 07:56 AM
[NMR paper] A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
Related Articles A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
J Biomol NMR. 2015 Feb 19;
Authors: Anderson KM, Nguyen D, Esadze A, Zandrashvili L, Gorenstein DG, Iwahara J
Abstract
Protein-nucleic acid interactions involve...
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02-19-2015 07:03 PM
[NMR paper] A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
Related Articles A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic Solids.
Isr J Chem. 2014 Feb 1;54(1-2):171-183
Authors: Hou G, Gupta R, Polenova T, Vega AJ
Abstract
Proton chemical shifts are a rich probe of structure and hydrogen bonding environments in organic and biological molecules. Until recently,...
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12-09-2014 01:13 PM
[NMR paper] Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Site-specific identification of an a? fibril-heparin interaction site by using solid-state 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 Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3
Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA
Abstract
At the...
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[NMR paper] Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.
Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.
Related Articles Site-specific interaction between ?-synuclein and membranes probed by NMR-observed methionine oxidation rates.
J Am Chem Soc. 2013 Feb 11;
Authors: Maltsev AS, Chen J, Levine RL, Bax A
Abstract
?-Synuclein (aS) is an intrinsically disordered protein that is water soluble but also can bind negatively charged lipid membranes while adopting an ?-helical conformation. Membrane affinity is increased by...