[NMR paper] Solid-state NMR and Membrane Proteins
Solid-state NMR and Membrane Proteins
Publication date: Available online 29 December 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Stanley J. Opella</br>
The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects solid-state...
[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
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07-09-2013 02:47 PM
[NMR paper] Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Acc Chem Res. 2013 May 10;
Authors: Tang M, Comellas G, Rienstra CM
Abstract
Solid-state NMR (SSNMR) spectroscopy has become an important technique for studying the biophysics and structure biology of proteins. This technique is especially useful for insoluble membrane proteins and amyloid fibrils, which are essential for...
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05-11-2013 10:26 PM
The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals
From The DNP-NMR Blog:
The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals
Banerjee, D., et al., The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals. J. Magn. Reson., 2013. 230(0): p. 212-219.
http://dx.doi.org/10.1016/j.jmr.2013.02.010
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05-07-2013 12:31 AM
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Eur Biophys J. 2011 Apr;40(4):447-62
Authors: Toke O, Bánóczi Z, Király P, Heinzmann R, Bürck J, Ulrich AS, Hudecz F
Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly...
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07-20-2011 10:00 AM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
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02-24-2011 11:04 AM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
BCL-2 Family Proteins Effect on Mitochondrial-Mimicking Membrane Structure by Solid State NMR
Linear Mode
