Related ArticlesMembrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy.
Biochim Biophys Acta Biomembr. 2020 May 01;:183333
Authors: Park SH, Wu J, Yao Y, Singh C, Tian Y, Marassi FM, Opella SJ
Abstract
Well-hydrated phospholipid bilayers provide a near-native environment for membrane proteins. They enable the preparation of chemically-defined samples suitable for NMR and other spectroscopic experiments that reveal the structure, dynamics, and functional interactions of the proteins at atomic resolution. The synthetic polymer styrene maleic acid (SMA) can be used to prepare detergent-free samples that form macrodiscs with diameters greater than 30 nm at room temperature, and spontaneously align in the magnetic field of an NMR spectrometer at temperatures above 35 °C. Here we show that magnetically aligned macrodiscs are particularly well suited for solid-state NMR experiments of membrane proteins because the SMA-lipid assembly both immobilizes the embedded protein and provides uniaxial order for oriented sample (OS) solid-state NMR studies. We show that aligned macrodiscs incorporating four different membrane proteins with a wide range of sizes and topological complexity yield high-resolution OS solid-state NMR spectra. The work is dedicated to Michelle Auger who made key contributions to the field of membrane and membrane protein biophysics.
PMID: 32371072 [PubMed - as supplied by publisher]
Magnetically Oriented Phospholipid Bilayer Discs for Membrane Protein NMR
Magnetically Oriented Phospholipid Bilayer Discs for Membrane Protein NMR
Publication date: 2 February 2018
Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1</br>
Author(s): Sang Ho Park, Jasmina Radoicic, Stanley J. Opella</br>
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02-07-2018 03:41 PM
[NMR paper] Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles.
Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles.
Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles.
J Magn Reson. 2015 Apr 28;256:14-22
Authors: Koroloff SN, Nevzorov AA
Abstract
Solid-state NMR (ssNMR) of oriented membrane proteins (MPs) is capable of providing...
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05-13-2015 02:01 PM
[NMR paper] Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles
Optimization of cross-polarization at low radiofrequency fields for sensitivity enhancement in solid-state NMR of membrane proteins reconstituted in magnetically aligned bicelles
Publication date: Available online 28 April 2015
Source:Journal of Magnetic Resonance</br>
Author(s): Sophie N. Koroloff , Alexander A. Nevzorov</br>
Solid-state NMR (ssNMR) of oriented membrane proteins (MPs) is capable of providing structural and dynamic information at nearly physiological conditions. However, NMR experiments performed on oriented membrane proteins generally suffer from...
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04-28-2015 12:40 PM
[NMR paper] Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
J Magn Reson. 2014 Mar 1;242C:224-232
Authors: Das BB, Zhang H, Opella SJ
Abstract
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of heteronuclear dipolar coupling...
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04-06-2014 02:01 AM
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of Rotationally Aligned Membrane Proteins in Phospholipid Bilayers
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of Rotationally Aligned Membrane Proteins in Phospholipid Bilayers
Publication date: Available online 1 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Bibhuti B. Das , Hua Zhang , Stanley J. Opella</br>
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of hetero-nuclear dipolar coupling frequencies in combination with conventional chemical shift based assignment methods is demonstrated. The...
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03-01-2014 11:11 AM
[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
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers
Abstract Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring 1H-15N dipolar couplings (DC) and 15N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal...
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[NMR paper] Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lantha
Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies.
Related Articles Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies.
Biochem Cell Biol. 1998;76(2-3):443-51
Authors: Prosser RS, Volkov VB, Shiyanovskaya IV
The addition of lanthanides (Tm3+, Yb3+, Er3+, or Eu3+) to a solution of long-chain phospholipids such as dimyristoylphosphatidylcholine (DMPC) and short-chain phospholipids such as...