Evidence map›Paper›PMID 23975771›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2013

Measuring transmembrane helix interaction strengths in lipid bilayers using steric trapping.

Heedeok Hong, Yu-Chu Chang, James U Bowie

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.6field-weighted citation impact, top 5% of its field
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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Membrane proteins enter the fold.Current opinion in structural biology · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Cholesterol as a co-solvent and a ligand for membrane proteins.Protein science : a publication of the Protein Society · 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

3 authors at 2 institutions in 1 country.

Heedeok HongDepartment of Chemistry, Michigan State University, East Lansing, MI, USA.
Yu-Chu Chang
James U Bowie
University of California, Los Angeles · USMichigan State University · US

Funding

Membrane Protein StabilityR01GM063919 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2001 to 2021
$5.6M
Improving membrane protein crystallizationR01GM081783 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2007 to 2009
$853k
NIGMS NIH HHS R01 GM063919NIGMS NIH HHS R01GM063919NIGMS NIH HHS R01 GM081783NIGMS NIH HHS R01GM081783
6 · The paper itself

Abstract

We have developed a method to measure strong transmembrane (TM) helix interaction affinities in lipid bilayers that are difficult to measure by traditional dilution methods. The method, called steric trapping, couples dissociation of biotinylated TM helices to a competitive binding by monovalent streptavidin (mSA), so that dissociation is driven by the affinity of mSA for biotin and mSA concentration. By adjusting the binding affinity of mSA through mutation, the method can obtain dissociation constants of TM helix dimers (K d,dimer) over a range of six orders of magnitudes. The K d,dimer limit of measurable target interaction is extended 3-4 orders of magnitude lower than possible by dilution methods. Thus, steric trapping opens up new opportunities to study the folding and assembly of α-helical membrane proteins in lipid bilayer environments. Here we provide detailed methods for applying steric trapping to a TM helix dimer.

Indexed as

Amino Acid SequenceBiotinylationCell MembraneLipid BilayersMembrane ProteinsMolecular Sequence DataProtein BindingProtein Interaction MappingProtein RefoldingProtein Structure, SecondaryProtein Structure, TertiaryProteolipidsPyrenesStreptavidinSulfhydryl CompoundsThermodynamicsLipid BilayersMembrane ProteinsProteolipidsproteoliposomespyrenePyrenesStreptavidinSulfhydryl Compounds

Identifiers

PMID23975771
PMCPMC4986992
OpenAlexW2396685905

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.