Evidence map›Paper›PMID 16371468›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7.

Joerg Gsponer, Harri Hopearuoho, Sara B-M Whittaker, Graham R Spence, Geoffrey R Moore, Emanuele Paci, Sheena E Radford, Michele Vendruscolo

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Native State of Complement Protein C3d Analysed via Hydrogen Exchange and Conformational Sampling.International journal of computational biology and drug design · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Biophysics of protein evolution and evolutionary protein biophysics.Journal of the Royal Society, Interface · 2014
    Article
  12. Article
  13. Article
  14. Folding of a large protein at high structural resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Protein hydrogen exchange: testing current models.Protein science : a publication of the Protein Society · 2012
    Article
  18. Article
  19. 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
  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.

Joerg GsponerDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Harri Hopearuoho
Sara B-M Whittaker
Graham R Spence
Geoffrey R Moore
Emanuele Paci
Sheena E Radford
Michele Vendruscolo

Funding

Biotechnology and Biological Sciences Research Council BBS/B/04803Biotechnology and Biological Sciences Research Council SF16972
6 · The paper itself

Abstract

We present a detailed structural characterization of the intermediate state populated during the folding and unfolding of the bacterial immunity protein Im7. We achieve this result by incorporating a variety of experimental data available for this species in molecular dynamics simulations. First, we define the structure of the exchange-competent intermediate state of Im7 by using equilibrium hydrogen-exchange protection factors. Second, we use this ensemble to predict Phi-values and compare the results with the experimentally determined Phi-values of the kinetic refolding intermediate. Third, we predict chemical-shift measurements and compare them with the measured chemical shifts of a mutational variant of Im7 for which the kinetic folding intermediate is the most stable state populated at equilibrium. Remarkably, we found that the properties of the latter two species are predicted with high accuracy from the exchange-competent intermediate that we determined, suggesting that these three states are characterized by a similar architecture in which helices I, II, and IV are aligned in a native-like, but reorganized, manner. Furthermore, the structural ensemble that we obtained enabled us to rationalize the results of tryptophan fluorescence experiments in the WT protein and a series of mutational variants. The results show that the integration of diverse sets of experimental data at relatively low structural resolution is a powerful approach that can provide insights into the structural organization of this conformationally heterogeneous three-helix intermediate with unprecedented detail and highlight the importance of both native and non-native interactions in stabilizing its structure.

Indexed as

Models, MolecularProtein FoldingBiophysical PhenomenaBiophysicsCarrier ProteinsEscherichia coli ProteinsFluorescenceKineticsMutationProtein ConformationSpectrum Analysis, RamanCarrier ProteinsE colicin-binding immunity protein Im7, E coliEscherichia coli Proteins

Identifiers

PMID16371468
PMCPMC1324994

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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.