Evidence map›Paper›PMID 12876322›Full record

ArticleProtein science : a publication of the Protein Society2003

Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange.

Lidia Cristian, James D Lear, William F DeGrado

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Design principles of the common Gly-X6-Gly membrane protein building block.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  4. Folding and misfolding of potassium channel monomers during assembly and tetramerization.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  17. Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. Method to measure strong protein-protein interactions in lipid bilayers using a steric trap.Proceedings of the National Academy of Sciences of the United States of America · 2010
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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 1 institution in 1 country.

Lidia CristianDepartment of Biochemistry & Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.
James D Lear
William F DeGrado
University of Pennsylvania · US

Funding

Structure of M2 Proton Channel from Influenza A VirusR01GM056423 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1997 to 2016
$4.5M
NIGMS NIH HHS GM 56423NIGMS NIH HHS R01 GM056423
6 · The paper itself

Abstract

Although progress has been made in understanding the thermodynamic stability of water-soluble proteins, our understanding of the folding of membrane proteins is at a relatively primitive level. A major obstacle to understanding the folding of membrane proteins is the discovery of systems in which the folding is in thermodynamic equilibrium, and the development of methods to quantitatively assess this equilibrium in micelles and bilayers. Here, we describe the application of disulfide cross-linking to quantitatively measure the thermodynamics of membrane protein association in detergent micelles. The method involves initiating disulfide cross-linking of a protein under reversible redox conditions in a thiol-disulfide buffer and quantitative assessment of the extent of cross-linking at equilibrium. The 19-46 alpha-helical transmembrane segment of the M2 protein from the influenza A virus was used as a model membrane protein system for this study. Previously it has been shown that transmembrane peptides from this protein specifically self-assemble into tetramers that retain the ability to bind to the drug amantadine. We used thiol-disulfide exchange to quantitatively measure the tetramerization equilibrium of this transmembrane protein in dodecylphosphocholine (DPC) detergent micelles. The association constants obtained agree remarkably well with those derived from analytical ultracentrifugation studies. The experimental method established herein should provide a broadly applicable tool for thermodynamic studies of folding, oligomerization and protein-protein interactions of membrane proteins.

Indexed as

Protein FoldingChromatography, High Pressure LiquidDisulfidesGlutathioneKineticsMembrane ProteinsMicellesOxidation-ReductionProtein Structure, QuaternarySulfhydryl CompoundsThermodynamicsUltracentrifugationDisulfidesGlutathioneMembrane ProteinsMicellesSulfhydryl Compounds

Identifiers

PMID12876322
PMCPMC2323959
OpenAlexW2089880603

What OpenQuestion holds

Textmetadata
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.