Evidence map›Paper›PMID 22004760›Full record

ArticleBiophysical journal2011

GB1 is not a two-state folder: identification and characterization of an on-pathway intermediate.

Angela Morrone, Rajanish Giri, Rudesh D Toofanny, Carlo Travaglini-Allocatelli, Maurizio Brunori, Valerie Daggett, Stefano Gianni

Abstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Context-Aware Hydrophobicity Modeling: HydroMap and FastHydroMap.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Residue level quantification of protein stability in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Engineered solubility tag for solution NMR of proteins.Protein science : a publication of the Protein Society · 2013
    Article
  12. Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Folding pathways of proteins with increasing degree of sequence identities but different structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. 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

7 authors.

Angela MorroneIstituto Pasteur-Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Università di Roma "La Sapienza", Rome, Italy.
Rajanish Giri
Rudesh D Toofanny
Carlo Travaglini-Allocatelli
Maurizio Brunori
Valerie Daggett
Stefano Gianni

Funding

MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR01GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 2000 to 2014
$3.9M
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR29GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 1995 to 1999
–
NIGMS NIH HHS GM50789NIGMS NIH HHS R01 GM050789NIGMS NIH HHS R29 GM050789
6 · The paper itself

Abstract

The folding pathway of the small α/β protein GB1 has been extensively studied during the past two decades using both theoretical and experimental approaches. These studies provided a consensus view that the protein folds in a two-state manner. Here, we reassessed the folding of GB1, both by experiments and simulations, and detected the presence of an on-pathway intermediate. This intermediate has eluded earlier experimental characterization and is distinct from the collapsed state previously identified using ultrarapid mixing. Failure to identify the presence of an intermediate affects some of the conclusions that have been drawn for GB1, a popular model for protein folding studies.

Indexed as

Protein FoldingBacterial ProteinsHydrogen-Ion ConcentrationKineticsMolecular Dynamics SimulationProtein ConformationThermodynamicsBacterial ProteinsIgG Fc-binding protein, Streptococcus

Identifiers

PMID22004760
PMCPMC3192981

What OpenQuestion holds

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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.