Related ArticlesSolid-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 dihexanoylphosphatidylcholine (DHPC) is known to result in a bilayer phase in which the average bilayer normal aligns parallel to an applied magnetic field. Lanthanide-doped bilayers have enormous potential for the study of membrane proteins by solid-state NMR, low-angle diffraction, and a variety of optical spectroscopic techniques. However, the addition of lanthanides poses certain challenges to the NMR spectroscopist: coexistence of an isotropic phase and hysteresis effects, direct binding of the paramagnetic ion to the peptide or protein of interest, and severe paramagnetic shifts and line broadening. Lower water concentrations and larger DMPC/DHPC ratios than those typically used in bicelles consistently yield a single oriented bilayer phase that is stable over a wide range of temperature (approximately 35-90 degrees C). Among the above choice of lanthanides, Yb3+ is found to give minimal paramagnetic shifts and line broadening at acceptably low concentrations necessary for alignment (i.e., Yb3+/DMPC mole ratios equal to or greater than 0.01). Finally, the addition of a phospholipid chelate, 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine--diethylenetriaminepent aacetic acid, is observed to significantly reduce paramagnetic broadening and presumably prevent direct association of the peptide with the lanthanide ions.
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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10-10-2011 06:27 AM
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Solid-State (19)F-NMR of Peptides in Native Membranes.
Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
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05-21-2011 07:51 PM
(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
J Magn Reson. 2011 Apr 9;
Authors: Lin EC, Opella SJ
(1)H-irradiation under mismatched Hartmann-Hahn conditions provides an alternative mechanism for carrying out (15)N/(13)C transfers in triple-resonance heteronuclear correlation spectroscopy...
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1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 9 April 2011</br>
Eugene C., Lin , Stanley J., Opella</br>
1H-irradiation under mismatched Hartmann-Hahn conditions provides an alternative mechanism for carrying out 15N/13C transfers in triple-resonance heteronuclear correlation spectroscopy (HETCOR) on stationary samples of single crystals and aligned samples of biopolymers, which...
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04-10-2011 12:52 PM
1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 9 April 2011</br>
Eugene C., Lin , Stanley J., Opella</br>
1H-irradiation under mismatched Hartmann-Hahn conditions provides an alternative mechanism for carrying out 15N/13C transfers in triple-resonance heteronuclear correlation spectroscopy (HETCOR) on stationary samples of single crystals and aligned samples of biopolymers, which...
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04-10-2011 12:42 PM
[NMR paper] Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structu
Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins.
Related Articles Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins.
J Magn Reson. 2003 Mar;161(1):64-9
Authors: Marassi FM, Crowell KJ
The preparation of oriented, hydration-optimized lipid bilayer samples, for NMR structure determination of membrane proteins, is described. The samples consist of planar phospholipid bilayers, containing membrane proteins, that...
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11-24-2010 09:01 PM
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
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10-22-2010 04:33 PM
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Biochemistry. 2010 Aug 30;
Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM
Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...