ArticleJournal of biomolecular NMR1999
Dilute spin-exchange assignment of solid-state NMR spectra of oriented proteins: acetylcholine M2 in bilayers.
Article in Journal of biomolecular NMR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Journal of biomolecular NMR · 2014Article
- Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.The journal of physical chemistry. B · 2013Article
- Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013Article
- A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles.Journal of biomolecular NMR · 2012Article
- Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers.Journal of biomolecular NMR · 2011Article
- A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- On the performance of spin diffusion NMR techniques in oriented solids: prospects for resonance assignments and distance measurements from separated local field experiments.The journal of physical chemistry. B · 2010Article
- A resonance assignment method for oriented-sample solid-state NMR of proteins.Journal of the American Chemical Society · 2010Article
- Continuity conditions and torsion angles from ssNMR orientational restraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Structure determination of membrane proteins by NMR spectroscopy.Chemical reviews · 2004Review
- A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.Biophysical journal · 2004Article
- Towards high-resolution solid-state NMR on large uniformly 15N- and [13C,15N]-labeled membrane proteins in oriented lipid bilayers.Journal of biomolecular NMR · 2002Article
- A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy.Biophysical journal · 2001Article
- Nuclear magnetic resonance of membrane-associated peptides and proteins.Methods in enzymology · 2001Review
- A solid-state NMR index of helical membrane protein structure and topology.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2000Article
- Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy.Biophysical journal · 1999Article
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Authors and funding
7 authors.
Funding
Abstract
The assignment of amide resonances in the two-dimensional PISEMA (Polarization Inversion with Spin Exchange at the Magic Angle) spectrum of uniformly 15N labeled M2 peptide corresponding to the channel-lining segment of the acetylcholine receptor in oriented phospholipid bilayers is described. The majority of the resonances were assigned through comparisons with spectra from selectively 15N labeled recombinant peptides and specifically 15N labeled synthetic peptides. Some resonances were assigned to specific amino acid residues by means of homonuclear 15N spin-exchange spectroscopy. A modification to the conventional spin-exchange pulse sequence that significantly shortens the length of the experiments by combining the intervals for 15N spin-exchange and 1H magnetization recovery is described.
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