(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 (HETCOR) on stationary samples of single crystals and aligned samples of biopolymers, which improve the efficiency especially when the direct (15)N-(13)C dipolar couplings are small. In many cases, the sensitivity is improved by taking advantage of the (13)C(?) labeled sites in peptides and proteins with (13)C detection. The similarities between experimental and simulated spectra demonstrate the validity of the recoupling mechanism and identify the potential for applying these experiments to virus particles or membrane proteins in phospholipid bilayers; however, further development is needed in order to derive quantitative distance and angular constraints from these measurements.
PMID: 21543244 [PubMed - as supplied by publisher]
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
Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Structure Determination in “Shiftless” Solid State NMR of Oriented Protein Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011</br>
Yuanyuan, Yin , Alexander A., Nevzorov</br>
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up structural...
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06-21-2011 03:40 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...
nmrlearner
Journal club
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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...
[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...