[NMR paper] Lipid- and substrate-induced conformational and dynamic changes in a glycosyltransferase involved in E. coli LPS synthesis revealed by 19F and 31P NMR
WaaG is a glycosyltransferase (GT) involved in the synthesis of the bacterial cell wall, and in Escherichia coli it catalyzes the transfer of a glucose moiety from the donor substrate UDP-glucose onto the nascent lipopolysaccharide (LPS) molecule which when completed constitutes the major component of the bacterium's outermost defenses. Similar to other GTs of the GT-B fold, having two Rossman-like domains connected by a short linker, WaaG is believed to undergo complex inter-domain motions as...
[NMR paper] Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR.
Biophys J. 2015 Jan 6;108(1):5-9
Authors: Marek A, Tang W, Milikisiyants S, Nevzorov AA, Smirnov AI
Abstract
Anodic aluminum oxide substrates with macroscopically aligned homogeneous nanopores of 80*nm in diameter enable two-dimensional, solid-state nuclear magnetic resonance studies of lipid-induced...
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Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR
Nanotube Array Method for Studying Lipid-Induced Conformational Changes of a Membrane Protein by Solid-State NMR
Publication date: 6 January 2015
Source:Biophysical Journal, Volume 108, Issue 1</br>
Author(s): Antonin Marek , Wenxing Tang , Sergey Milikisiyants , Alexander*A. Nevzorov , Alex*I. Smirnov</br>
Anodic aluminum oxide substrates with macroscopically aligned homogeneous nanopores of 80*nm in diameter enable two-dimensional, solid-state nuclear magnetic resonance studies of lipid-induced conformational changes of uniformly 15N-labeled Pf1 coat protein...
[NMR paper] The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by 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 The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
Chemistry. 2014 Mar 13;
Authors: Schmidt P, Thomas L, Müller P, Scheidt HA, Huster D
Abstract
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[NMR paper] Combined NMR and GC-MS Analyses Revealed Dynamic Metabolic Changes Associated with the Carrageenan-induced Rat Pleurisy.
Combined NMR and GC-MS Analyses Revealed Dynamic Metabolic Changes Associated with the Carrageenan-induced Rat Pleurisy.
Related Articles Combined NMR and GC-MS Analyses Revealed Dynamic Metabolic Changes Associated with the Carrageenan-induced Rat Pleurisy.
J Proteome Res. 2013 Oct 17;
Authors: Li H, An Y, Zhang L, Lei H, Zhang L, Wang Y, Tang H
Abstract
Inflammation is closely associated with pathogenesis of various metabolic disorders, cardiovascular diseases and cancers. To understand the systems responses to localized inflammation, we...
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10-18-2013 06:23 PM
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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03-03-2011 12:34 PM
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....
Lipid- and substrate-induced conformational and dynamic changes in a glycosyltransferase involved in E. coli LPS synthesis revealed by 19F and 31P NMR
Linear Mode
