ArticleBiophysical journal2008
Helix conformations in 7TM membrane proteins determined using oriented-sample solid-state NMR with multiple residue-specific 15N labeling.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Assignment of oriented sample NMR resonances from a three transmembrane helix protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Broadband Heteronuclear Solid-State NMR Experiments by Exponentially Modulated Dipolar Recoupling without Decoupling.The journal of physical chemistry letters · 2010Article
- Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles.Biophysical journal · 2009Article
- Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.Journal of the American Chemical Society · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oriented solid-state NMR in combination with multiple-residue-specific (15)N labeling and extensive numerical spectral analysis is proposed to determine helix conformations of large membrane proteins in native membranes. The method is demonstrated on uniaxially oriented samples of (15)N-methionine, -valine, and -glycine-labeled bacteriorhopsin in native purple membranes. Experimental two-dimensional (1)H-(15)N dipole-dipole coupling versus (15)N chemical shift spectra for all samples are analyzed numerically to establish combined constraints on the orientation of the seven transmembrane helices relative to the membrane bilayer normal. Since the method does not depend on specific resonance assignments and proves robust toward nonidealities in the sample alignment, it may be generally feasible for the study of conformational arrangement and function-induced conformation changes of large integral membrane proteins.
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