ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2014
Assignment of oriented sample NMR resonances from a three transmembrane helix protein.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE.Nature communications · 2024Article
- A kink in DWORF helical structure controls the activation of the sarcoplasmic reticulum CaStructure (London, England : 1993) · 2022Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Detergent optimized membrane protein reconstitution in liposomes for solid state NMR.Biochemistry · 2014Article
- Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.Biophysical journal · 2014Article
- Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies.Frontiers in molecular biosciences · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Oriented sample solid state NMR techniques have been routinely employed to determine the structures of membrane proteins with one or two transmembrane helices. For larger proteins the technique has been limited by spectral resolution and lack of assignment strategies. Here, a strategy for resonance assignment is devised and applied to a three transmembrane helix protein. Sequence specific assignments for all labeled transmembrane amino acid sites are obtained, which provide a set of orientational restraints and helix orientations in the bilayer. Our experiments expand the utility of solid state NMR in membrane protein structure characterization to three transmembrane helix proteins and represent a straightforward strategy for routinely characterizing multiple transmembrane helix protein structures.
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