Publication date: Available online 12 July 2017 Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Author(s): Vladimir Ladizhansky
Membrane proteins mediate flow of molecules, signals, and energy between cells and intracellular compartments. Understanding membrane protein function requires a detailed understanding of the structural and dynamic properties involved. Lipid bilayers provide a native-like environment for structure-function investigations of membrane proteins. In this review we give a general discourse on the recent progress in the field of solid-state NMR of membrane proteins. Solid-state NMR is a variation of NMR spectroscopy that is applicable to molecular systems with restricted mobility, such as high molecular weight proteins and protein complexes, supramolecular assemblies, or membrane proteins in a phospholipid environment. We highlight recent advances in applications of solid-state NMR to membrane proteins, specifically focusing on the recent developments in the field of Dynamic Nuclear Polarization, proton detection, and solid-state NMR applications in situ (in cell membranes). This article is part of a Special Issue entitled: Biophysics in Canada, edited by Lewis Kay, John Baenziger, Albert Berghuis and Peter Tieleman. Graphical abstract
[NMR paper] Solid-state NMR structures of integral membrane proteins.
Solid-state NMR structures of integral membrane proteins.
Related Articles Solid-state NMR structures of integral membrane proteins.
Mol Membr Biol. 2016 Feb 8;:1-23
Authors: Patching SG
Abstract
Solid-state NMR is unique for its ability to obtain three-dimensional structures and to measure atomic-resolution structural and dynamic information for membrane proteins in native lipid bilayers. An increasing number and complexity of integral membrane protein structures have been determined by solid-state NMR using two main methods....
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02-10-2016 09:28 PM
[NMR paper] REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.
J Magn Reson. 2015 Apr;253:154-65
Authors: Jia L, Liang S, Sackett K, Xie L, Ghosh U, Weliky DP
Abstract
Rotational-echo double-resonance (REDOR) solid-state NMR is applied to probe the membrane...
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03-24-2015 09:58 PM
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins
REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Lihui Jia , Shuang Liang , Kelly Sackett , Li Xie , Ujjayini Ghosh , David P. Weliky</br>
Rotational-echo double-resonance (REDOR) solid-state NMR is applied to probe the membrane locations of specific residues of membrane proteins. Couplings are measured between protein 13CO nuclei and membrane lipid or cholesterol 2H and 31P nuclei. Specific 13CO labeling is used...
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03-20-2015 01:48 AM
[NMR paper] Solid-state NMR and membrane proteins.
Solid-state NMR and membrane proteins.
Related Articles Solid-state NMR and membrane proteins.
J Magn Reson. 2014 Dec 29;
Authors: Opella SJ
Abstract
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...
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02-16-2015 04:43 PM
[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...
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12-30-2014 03:28 PM
Perspectives in Enzymology of Membrane Proteins by Solid-State NMR
From The DNP-NMR Blog:
Perspectives in Enzymology of Membrane Proteins by Solid-State NMR
Ullrich, S.J. and C. Glaubitz, Perspectives in Enzymology of Membrane Proteins by Solid-State NMR. Acc. Chem. Res., 2013.
http://dx.doi.org/10.1021/ar4000289
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08-12-2013 03:27 PM
[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...
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12-01-2010 06:56 PM
Solid State NMR of membrane peptides and proteins
Solid State NMR of membrane peptides and proteins
Lecture notes on "Solid State NMR of membrane peptides and proteins" by Dr. SK Straus from Univ. of British Columbia
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Applications of solid-state NMR to membrane proteins
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