[NMR paper] Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 12;
Authors: Gayen A, Banigan JR, Traaseth NJ
Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms...
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Lenica Reggie, Jakob J. Lopez, Ian Collinson, Clemens Glaubitz and Mark Lorch
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209378h/aop/images/medium/ja-2011-09378h_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209378h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/e6Ae3MMc0OU
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[NMR paper] NMR and fluorescence spectroscopy approaches to secondary and primary active multidrug efflux pumps.
NMR and fluorescence spectroscopy approaches to secondary and primary active multidrug efflux pumps.
Related Articles NMR and fluorescence spectroscopy approaches to secondary and primary active multidrug efflux pumps.
Biochem Soc Trans. 2005 Aug;33(Pt 4):873-7
Authors: Lorch M, Lehner I, Siarheyeva A, Basting D, Pfleger N, Manolikas T, Glaubitz C
Multidrug efflux pumps are found in all major transporter families. Along with a lack of three-dimensional structure information, the mechanism of drug recognition, energy coupling with drug...
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12-01-2010 06:56 PM
[NMR paper] Polarization of cinnamoyl-CoA substrates bound to enoyl-CoA hydratase: correlation of
Polarization of cinnamoyl-CoA substrates bound to enoyl-CoA hydratase: correlation of (13)C NMR with quantum mechanical calculations and calculation of electronic strain energy.
Related Articles Polarization of cinnamoyl-CoA substrates bound to enoyl-CoA hydratase: correlation of (13)C NMR with quantum mechanical calculations and calculation of electronic strain energy.
Biochemistry. 2002 Feb 26;41(8):2630-40
Authors: D'Ordine RL, Pawlak J, Bahnson BJ, Anderson VE
When alpha,beta-unsaturated substrates bind to the active site of enoyl-CoA...
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[NMR paper] Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state
Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.
Related Articles Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.
Biophys J. 2002 Feb;82(2):1017-29
Authors: Hatcher ME, Hu JG, Belenky M, Verdegem P, Lugtenburg J, Griffin RG, Herzfeld J
By varying the pH, the D85N mutant of bacteriorhodopsin provides models for several photocycle intermediates of the wild-type protein in which D85 is protonated. At pH 10.8, NMR spectra of...
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[NMR paper] 31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein E
31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE.
Related Articles 31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE.
FEBS Lett. 2000 Sep 1;480(2-3):127-31
Authors: Glaubitz C, Gröger A, Gottschalk K, Spooner P, Watts A, Schuldiner S, Kessler H
The binding of tetraphenylphosphonium (TPP+) to EmrE, a membrane-bound, 110 residue Escherichia coli multidrug transport protein, has been observed by 31P cross-polarisation-magic-angle spinning nuclear magnetic resonance...
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11-19-2010 08:29 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...