Evidence map›Paper›PMID 19425578›Full record

ArticleJournal of the American Chemical Society2009

Mixing and matching detergents for membrane protein NMR structure determination.

Linda Columbus, Jan Lipfert, Kalyani Jambunathan, Daniel A Fox, Adelene Y L Sim, Sebastian Doniach, Scott A Lesley

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Low- q Bicelles Are Mixed Micelles.The journal of physical chemistry letters · 2018
    Article
  10. Bicelle size modulates the rate of bacteriorhodopsin folding.Protein science : a publication of the Protein Society · 2018
    Article
  11. Article
  12. Review
  13. Article
  14. Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Membrane proteins, detergents and crystals: what is the state of the art?Acta crystallographica. Section F, Structural biology communications · 2014
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Linda ColumbusDepartment of Chemistry, University of Virginia, Charlottesville, Virginia 22904, USA. Columbus@virginia.edu
Jan Lipfert
Kalyani Jambunathan
Daniel A Fox
Adelene Y L Sim
Sebastian Doniach
Scott A Lesley

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
JOINT CENTER FOR STRUCTURAL GENOMICSP50GM062411 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WILSON, IAN A · 2000 to 2004
$32.9M
Time-resolved small angle X-ray scatteringP01GM066275 · NIGMS · STANFORD UNIVERSITY · PI HERSCHLAG, DANIEL · 2003 to 2017
$17.8M
NMR Structure of Membrane Proteins of T. maritimaF32GM068286 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI COLUMBUS, LINDA M · 2003 to 2005
$139k
NIGMS NIH HHS 1F32GM068286NIGMS NIH HHS F32 GM068286NIGMS NIH HHS P01 GM0066275NIGMS NIH HHS P01 GM066275NIGMS NIH HHS P50 GM062411NIGMS NIH HHS P50 GM62411NIGMS NIH HHS U54 GM074898
6 · The paper itself

Abstract

One major obstacle to membrane protein structure determination is the selection of a detergent micelle that mimics the native lipid bilayer. Currently, detergents are selected by exhaustive screening because the effects of protein-detergent interactions on protein structure are poorly understood. In this study, the structure and dynamics of an integral membrane protein in different detergents is investigated by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy and small-angle X-ray scattering (SAXS). The results suggest that matching of the micelle dimensions to the protein's hydrophobic surface avoids exchange processes that reduce the completeness of the NMR observations. Based on these dimensions, several mixed micelles were designed that improved the completeness of NMR observations. These findings provide a basis for the rational design of mixed micelles that may advance membrane protein structure determination by NMR.

Indexed as

DetergentsMembrane ProteinsMicellesNuclear Magnetic Resonance, BiomolecularProtein ConformationDetergentsMembrane ProteinsMicelles

Identifiers

PMID19425578
PMCPMC2751809

What OpenQuestion holds

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Registered trials

None linked

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.