Structure determination of aligned systems by solid-state NMR magic angle spinning methods

Gross, Ben; Tanski, Joseph M.; McDermott, Ann E.

doi:10.1016/j.jmr.2005.06.008

Cited by 4 publications

(1 citation statement)

References 31 publications

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“…chemical shift and heteronuclear dipolar coupling frequencies) measured in separated local field [21] and other high-resolution solidstate NMR experiments. This information can be obtained not only for immobile systems but also in MAS studies of oriented samples [24,25]. The structures of gramicidin [26], the transmembrane M2 domain of the acetylcholine receptor [27], the transmembrane domain of the M2 protein from the influenza A virus [28], the membrane-bound form of coat protein [29], the transmembrane domain of Vpu [30], and the mercury transport membrane protein MerFt [31] have been obtained in bilayers mechanically aligned on glass plates or in magnetically aligned bicelles [32,33].…”

Section: Introductionmentioning

confidence: 99%

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples

Nevzorov

Opella

2007

Journal of Magnetic Resonance

142

147

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Section: Introductionmentioning

confidence: 99%

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples

Nevzorov

Opella

2007

Journal of Magnetic Resonance

142

147

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Separated local field NMR experiments on oriented samples rotating at the magic angle

Lopez

Mason²,

Kaiser

et al. 2006

J Biomol NMR

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Biophysical studies on membrane proteins by solid state NMR (SSNMR) can be carried out directly in a membrane environment. Samples are usually prepared in form of multi-lamellar dispersions for magic angle sample spinning or as aligned multi-layers for orientation dependent NMR experiments without sample rotation. A new development is the application of MAS NMR to aligned samples (MAOSS; Magic Angle Oriented Sample Spinning). In combination with separated local field (SLF) experiments, size and orientation of heteronuclear dipolar couplings may be extracted from two-dimensional experiments which correlate dipolar couplings with isotropic chemical shifts. The orientation of these (1)H-X dipolar couplings can be directly related to the orientation of molecular groups in the sample. Here, we demonstrate the feasibility of these experiments on highly ordered polyethylene fibers which serve as model compound. Based on these data, the experiment is also applied to ordered multi-layers of bacteriorhodopsin (purple membrane) which is used as a model for aligned membrane proteins. We present a detailed analysis of different experimental designs with respect to angular sensitivity and the influence of residual sample disorder ("mosaic spread"). The results of the MAOSS-SLF experiment are discussed within the context of established solid state NMR experiments which are usually performed without sample rotation and we compare the data to orientation information obtained from X-ray diffraction.

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Applications of REDOR for Distance Measurements in Biological Solids

Grage¹,

Watts

2006

Annual Reports on NMR Spectroscopy

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Structure determination of aligned systems by solid-state NMR magic angle spinning methods

Cited by 4 publications

References 31 publications

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples

Separated local field NMR experiments on oriented samples rotating at the magic angle

Applications of REDOR for Distance Measurements in Biological Solids

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