Evidence map›Paper›PMID 11916873›Full record

ArticleBiophysical journal2002

Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins.

Gianluigi Veglia, Ana Carolina Zeri, Che Ma, Stanley J Opella

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
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  7. Article
  8. Review
  9. Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Article
  12. Review
  13. NMR studies of p7 protein from hepatitis C virus.European biophysics journal : EBJ · 2010
    Article
  14. Article
  15. Interaction and conformational dynamics of membrane-spanning protein helices.Protein science : a publication of the Protein Society · 2009
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

4 authors at 2 institutions in 1 country.

Gianluigi VegliaDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Ana Carolina Zeri
Che Ma
Stanley J Opella
University of California San Diego · USUniversity of Minnesota · US

Funding

STRUCTURE DETERMINATION OF VPU FROM HIV 1P01GM056538 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI MONTAL, MAURICIO S · 1997 to 2002
$1.6M
SOLID-STATE NMR OF PEPTIDESR01GM029754 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OPELLA, STANLEY J · 1985 to 2002
$670k
NIGMS NIH HHS P01 GM56538NIGMS NIH HHS R01 GM29754
6 · The paper itself

Abstract

Deuterium/hydrogen exchange factors (chi) were measured for the backbone amide sites of the membrane-bound forms of the 50-residue fd coat protein and the 23-residue magainin2 peptide in lipid micelles by solution nuclear magnetic resonance spectroscopy. By combining kinetic and thermodynamic effects, deuterium/hydrogen exchange factors overcome the principal limitations encountered in the measurements of kinetic protection factors and thermodynamic fractionation factors for membrane proteins. The magnitudes of the exchange factors can be correlated with the structure and topology of membrane-associated polypeptides. In fd coat protein, residues in the transmembrane helix have exchange factors that are substantially smaller than those in the amphipathic surface helix or the loop connecting the two helices. For the amphipathic helical peptide, magainin2, the exchange factors of residues exposed to the solvent are appreciably larger than those that face the hydrocarbon portion of membrane bilayers. These examples demonstrate that deuterium/hydrogen exchange factors can be measured by solution NMR spectroscopy and used to identify residues in transmembrane helices as well as to determine the polarity of amphipathic helices in membrane proteins.

Indexed as

Xenopus ProteinsAntimicrobial Cationic PeptidesBiophysical PhenomenaBiophysicsCell MembraneDeuteriumHydrogenHydrogen-Ion ConcentrationKineticsLipid BilayersMagaininsMagnetic Resonance SpectroscopyMicellesModels, BiologicalSpectrophotometryThermodynamicsAntimicrobial Cationic PeptidesDeuteriumHydrogenLipid Bilayersmagainin 2 peptide, XenopusMagaininsMicellesXenopus Proteins

Identifiers

PMID11916873
PMCPMC1302011
OpenAlexW2064034935

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.