Publication date: Available online 6 October 2014 Source:Journal of Magnetic Resonance
Author(s): Alexander A. Nevzorov
A new approach for calculating solid-state NMR lineshapes of uniaxially rotating membrane proteins under the magic-angle spinning conditions is presented. The use of stochastic Liouville equation (SLE) allows one to account for both coherent sample rotation and stochastic motional averaging of the spherical dipolar powder patterns by uniaxial diffusion of the spin-bearing molecules. The method is illustrated via simulations of the dipolar powder patterns of rigid samples under the MAS conditions, as well as the recent method of rotational alignment in the presence of both MAS and rotational diffusion under the conditions of dipolar recoupling. It has been found that it is computationally more advantageous to employ direct integration over a spherical grid rather than to use a full angular basis set for the SLE solution. Accuracy estimates for the bond angles measured from the recoupled amide 1H-15N dipolar powder patterns have been obtained at various rotational diffusion coefficients. It has been shown that the rotational alignment method is applicable to membrane proteins approximated as cylinders with radii of approximately 20 Ĺ, for which uniaxial rotational diffusion within the bilayer is sufficiently fast and exceeds the rate 2×105 s-1. Graphical abstract
Evidence for Coherent Transfer of para-Hydrogen-Induced Polarization at Low Magnetic Fields
From The DNP-NMR Blog:
Evidence for Coherent Transfer of para-Hydrogen-Induced Polarization at Low Magnetic Fields
Kiryutin, A.S., et al., Evidence for Coherent Transfer of para-Hydrogen-Induced Polarization at Low Magnetic Fields. The Journal of Physical Chemistry Letters, 2013. 4(15): p. 2514-2519.
http://dx.doi.org/10.1021/jz401210m
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11-21-2013 01:14 AM
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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11-16-2013 03:14 PM
The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals
From The DNP-NMR Blog:
The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals
Banerjee, D., et al., The interplay between the solid effect and the cross effect mechanisms in solid state 13C DNP at 95 GHz using trityl radicals. J. Magn. Reson., 2013. 230(0): p. 212-219.
http://dx.doi.org/10.1016/j.jmr.2013.02.010
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05-07-2013 12:31 AM
[NMR paper] Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms.
Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms.
Related Articles Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms.
Magn Reson Chem. 2007 Dec;45 Suppl 1:S161-73
Authors: Skrynnikov NR
Abstract
It has been long noted that J-resolved doublets observed in solid-state MAS experiments are asymmetric. The asymmetry has been attributed to a coherent interference effect involving dipolar and CSA interactions. Recently, Bernd Reif and co-workers suggested that under fast MAS conditions the coherent portion...
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04-03-2013 08:22 PM
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Revealing Protein Structures in Solid-Phase Peptide Synthesis by 13C Solid-State NMR: Evidence of Excessive Misfolding for Alzheimer’s ?
Songlin Wang and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja212190z/aop/images/medium/ja-2011-12190z_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja212190z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6EE7uthrnLg
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
Coherent and Stochastic Averaging in Solid-State NMR
Linear Mode
