Identificationof Dynamic Modes in an IntrinsicallyDisordered Protein Using Temperature-Dependent NMR Relaxation
Identificationof Dynamic Modes in an IntrinsicallyDisordered Protein Using Temperature-Dependent NMR Relaxation
Anton Abyzov, Nicola Salvi, Robert Schneider, Damien Maurin, Rob W.H. Ruigrok, Malene Ringkjøbing Jensen and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02424/20160506/images/medium/ja-2016-02424a_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02424
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05-07-2016 03:19 AM
[NMR paper] Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Related Articles Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
J Am Chem Soc. 2016 Apr 26;
Authors: Abyzov A, Salvi N, Schneider R, Maurin D, Ruigrok RW, Jensen MR, Blackledge M
Abstract
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04-27-2016 01:51 PM
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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01-30-2016 07:56 AM
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Protein resonance assignment at MAS frequencies approaching 100Â*kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
Abstract
We discuss the optimum experimental conditions to obtain assignment spectra for solid proteins at magic-angle spinning (MAS) frequencies around 100Â*kHz. We present a systematic examination of the MAS dependence of the amide proton T 2â?² times and a site-specific comparison of T 2â?² at 93Â*kHz versus 60Â*kHz MAS frequency. A...
Dynamic Nuclear Polarization Study of Inhibitor Binding to the M218-60 Proton Transporter from Influenza A
From the The DNP-NMR Blog:
Dynamic Nuclear Polarization Study of Inhibitor Binding to the M218-60 Proton Transporter from Influenza A
Andreas, L.B., et al., Dynamic Nuclear Polarization Study of Inhibitor Binding to the M218-60 Proton Transporter from Influenza A. Biochemistry, 2013.
http://www.ncbi.nlm.nih.gov/pubmed/23480101
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04-15-2013 08:52 AM
[NMR paper] Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Related Articles Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Anal Bioanal Chem. 2004 Aug;379(7-8):1045-9
Authors: Nissler L, Gebhardt R, Berger S
Flavonoids are well known to inhibit the function of the multi-drug-resistance (mdr) transporter by interacting with their ATP binding domains. The precise orientation of these molecules inside the ATP binding pocket is still unclear. We applied the saturation transfer...
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11-24-2010 09:51 PM
[NMR paper] NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
Related Articles NMR investigation of the multidrug transporter EmrE, an integral membrane protein.
Eur J Biochem. 1998 Jun 15;254(3):610-9
Authors: Schwaiger M, Lebendiker M, Yerushalmi H, Coles M, Gröger A, Schwarz C, Schuldiner S, Kessler H
EmrE is an Escherichia coli multidrug transport protein that confers resistance to a wide range of toxicants by active transport across the bacterial cell membrane. The highly hydrophobic polytopic integral membrane...