Evidence map›Paper›PMID 9194192›Full record

ArticleProtein science : a publication of the Protein Society1997

Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.

E W Chung, E J Nettleton, C J Morgan, M Gross, A Miranker, S E Radford, C M Dobson, C V Robinson

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.5field-weighted citation impact, top 1% 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

22 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Double superhelix model of high density lipoprotein.The Journal of biological chemistry · 2009
    Article
  7. The gramicidin dimer shows both EX1 and EX2 mechanisms of H/D exchange.Journal of the American Society for Mass Spectrometry · 2009
    Article
  8. Scope and utility of hydrogen exchange as a tool for mapping landscapes.Protein science : a publication of the Protein Society · 2007
    Article
  9. Article
  10. Article
  11. Article
  12. Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  13. Structural features of interferon-gamma aggregation revealed by hydrogen exchange.Protein science : a publication of the Protein Society · 2002
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Folding of a three-stranded coiled coil.Protein science : a publication of the Protein Society · 2000
    Article
  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

8 authors at 1 institution in 1 country.

E W ChungOxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, United Kingdom.
E J Nettleton
C J Morgan
M Gross
A Miranker
S E Radford
C M Dobson
C V Robinson
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The extent of deuterium labeling of hen lysozyme, its three-disulfide derivative, and the homologous alpha-lactalbumins, has been measured by both mass spectrometry and NMR. Different conformational states of the proteins were produced by varying the solution conditions. Alternate protein conformers were found to contain different numbers of 2H atoms. Furthermore, measurement in the gas phase of the mass spectrometer or directly in solution by NMR gave consistent results. The unique ability of mass spectrometry to distinguish distributions of 2H atoms in protein molecules is exemplified using samples prepared to contain different populations of 2H-labeled protein. A comparison of the peak widths of bovine alpha-lactalbumin in alternate solution conformations but containing the same average number of 2H atoms showed dramatic differences due to different 2H distributions in the two protein conformers. Measurement of 2H distributions by ESI-MS enabled characterization of conformational averaging and structural heterogeneity. In addition, a time course for hydrogen exchange was examined and the variation in distributions of 2H atom compared with simulations for different hydrogen exchange models. The results clearly show that exchange from the native state of bovine alpha-lactalbumin at 15 degrees C is dominated by local unfolding events.

Indexed as

ProtonsAnimalsCattleChickensDeuteriumIsotope LabelingLactalbuminMagnetic Resonance SpectroscopyMass SpectrometryMuramidaseProtein ConformationProtein DenaturationSolutionsDeuteriumLactalbuminMuramidaseProtonsSolutions

Identifiers

PMID9194192
PMCPMC2143718
OpenAlexW2120977203

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.