Evidence map›Paper›PMID 21976256›Full record

ArticleJournal of biomolecular NMR2011

Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers.

Kaustubh R Mote, T Gopinath, Nathaniel J Traaseth, Jason Kitchen, Peter L Gor'kov, William W Brey, Gianluigi Veglia

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Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

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0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 3D MAS NMR Experiment Utilizing Through-SpaceJournal of the American Chemical Society · 2017
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Assignment of oriented sample NMR resonances from a three transmembrane helix protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  17. Review
  18. Review
  19. Article
  20. Review
4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Kaustubh R MoteDepartment of Chemistry, University of Minnesota, Minneapolis, MN 55455-0431, USA.
T Gopinath
Nathaniel J Traaseth
Jason Kitchen
Peter L Gor'kov
William W Brey
Gianluigi Veglia

Funding

NMR Structural Analysis of Calcium Regulation in MuscleR01GM064742 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI VEGLIA, GIANLUIGI · 2002 to 2019
$7.1M
NIGMS NIH HHS GM 64742
6 · The paper itself

Abstract

Oriented solid-state NMR is the most direct methodology to obtain the orientation of membrane proteins with respect to the lipid bilayer. The method consists of measuring (1)H-(15)N dipolar couplings (DC) and (15)N anisotropic chemical shifts (CSA) for membrane proteins that are uniformly aligned with respect to the membrane bilayer. A significant advantage of this approach is that tilt and azimuthal (rotational) angles of the protein domains can be directly derived from analytical expression of DC and CSA values, or, alternatively, obtained by refining protein structures using these values as harmonic restraints in simulated annealing calculations. The Achilles' heel of this approach is the lack of suitable experiments for sequential assignment of the amide resonances. In this Article, we present a new pulse sequence that integrates proton driven spin diffusion (PDSD) with sensitivity-enhanced PISEMA in a 3D experiment ([(1)H,(15)N]-SE-PISEMA-PDSD). The incorporation of 2D (15)N/(15)N spin diffusion experiments into this new 3D experiment leads to the complete and unambiguous assignment of the (15)N resonances. The feasibility of this approach is demonstrated for the membrane protein sarcolipin reconstituted in magnetically aligned lipid bicelles. Taken with low electric field probe technology, this approach will propel the determination of sequential assignment as well as structure and topology of larger integral membrane proteins in aligned lipid bilayers.

Indexed as

AnisotropyLipid BilayersMembrane ProteinsModels, MolecularNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularLipid BilayersMembrane ProteinsNitrogen Isotopes

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.