scholarly journals Triton X-100 as the “Short-Chain Lipid” Improves the Magnetic Alignment and Stability of Membrane Proteins in Phosphatidylcholine Bilayers for Oriented-Sample Solid-State NMR Spectroscopy

2010 ◽  
Vol 132 (36) ◽  
pp. 12552-12553 ◽  
Author(s):  
Sang Ho Park ◽  
Stanley J. Opella
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Short Chain ◽  
Magnetic Alignment ◽  
Oriented Sample ◽  
Solid State Nmr Spectroscopy ◽  
Triton X

scholarly journals Magnetic-Alignment of Polymer Nanodiscs Probed by Solid-State NMR Spectroscopy

2019 ◽  
Author(s):  
Thirupathi Ravula ◽  
JaeWoong Kim ◽  
Dong-Kuk Lee ◽  
Ayyalusamy Ramamoorthy
Keyword(s):  
Magnetic Field ◽  
Solid State ◽  
Nmr Spectroscopy ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Field Direction ◽  
Magnetic Alignment ◽  
Magnetic Field Direction ◽  
Solid State Nmr Spectroscopy ◽  
The Magnetic Field

AbstractThe ability of amphipathic polymers to self-assemble with lipids and form nanodiscs has been a boon for the field of functional reconstitution of membrane proteins. In a field dominated by detergent micelles, a unique feature of polymer nanodiscs is their much-desired ability to align in the presence of an external magnetic field. Magnetic alignment facilitates the application of solid-state NMR spectroscopy and aids in the measurement of residual dipolar couplings (RDCs) via well-established solution NMR spectroscopy. In this study, we comprehensively investigate the magnetic-alignment properties of SMA-QA polymer based nanodiscs by using 31P and 14N solid-state NMR experiments under static conditions. The results reported herein demonstrate the spontaneous magnetic-alignment of large-size (≥ 20 nm diameter) SMA-QA nanodiscs (also called as macro-nanodiscs) with the lipid-bilayer-normal perpendicular to the magnetic field direction. Consequently, the orientation of macro-nanodiscs are further shown to flip their alignment axis parallel to the magnetic field direction upon the addition of a paramagnetic lanthanide salt. These results demonstrate the use of SMA-QA polymer nanodiscs for solid-state NMR applications including structural studies on membrane proteins.

scholarly journals Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments

Structure ◽  
2018 ◽  
Vol 26 (1) ◽  
pp. 161-170.e3 ◽  
Author(s):  
Lindsay A. Baker ◽  
Tessa Sinnige ◽  
Pascale Schellenberger ◽  
Jeanine de Keyzer ◽  
C. Alistair Siebert ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy ◽  
Electron Cryotomography
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