Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I
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03-02-2011 02:01 AM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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02-16-2011 07:40 PM
[NMR paper] NMR structure of Mistic, a membrane-integrating protein for membrane protein expressi
NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Related Articles NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Science. 2005 Feb 25;307(5713):1317-21
Authors: Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S
Although structure determination of soluble proteins has become routine, our understanding of membrane proteins has been limited by experimental bottlenecks in obtaining both sufficient yields of protein and ordered crystals. Mistic is an...
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11-24-2010 11:14 PM
[NMR paper] Solid-state NMR spectroscopic studies of an integral membrane protein inserted into a
Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays.
Related Articles Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays.
J Am Chem Soc. 2004 Aug 11;126(31):9504-5
Authors: Lorigan GA, Dave PC, Tiburu EK, Damodaran K, Abu-Baker S, Karp ES, Gibbons WJ, Minto RE
This communication demonstrates for the first time that solid-state NMR spectroscopic studies can be used to investigate aligned...
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11-24-2010 10:01 PM
[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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08-21-2010 11:12 PM
[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...
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08-21-2010 11:12 PM
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Jakob J. Lopez, Christoph Kaiser, Sarika Shastri and Clemens Glaubitz
Journal of Biomolecular NMR; 2008; 41(2) pp 97 - 104
Abstract:
13C homonuclear correlation spectra based on proton driven spin diffusion (PDSD) are becoming increasingly important for obtaining distance constraints from multiply labeled biomolecules by MAS NMR. One particular challenging situation arises when such constraints are to be obtained from spectra with a large natural abundance signal background which...