Evidence map›Paper›PMID 18644380›Full record

ArticleJournal of molecular biology2008

Subdomain competition, cooperativity, and topological frustration in the folding of CheY.

Ronald D Hills, Charles L Brooks

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 55 citations in OpenAlex.

  1. Structures of permuted halves of a modern ribose-binding protein.Acta crystallographica. Section D, Structural biology · 2023
    Article
  2. Article
  3. Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  5. Frustration and folding of a TIM barrel protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Sequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Evolution of a protein folding nucleus.Protein science : a publication of the Protein Society · 2016
    Article
  13. Conformational frustration in calmodulin-target recognition.Journal of molecular recognition : JMR · 2015
    Article
  14. Article
  15. Modulation of frustration in folding by sequence permutation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Binding and folding of the small bacterial chaperone HdeA.The journal of physical chemistry. B · 2013
    Article
  18. Article
  19. De novo prediction of protein folding pathways and structure using the principle of sequential stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

2 authors at 1 institution in 1 country.

Ronald D HillsDepartment of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, TPC6, La Jolla, CA 92037, USA.
Charles L Brooks
Scripps Research Institute · US

Funding

WEB BASED DOCUMENTATION &TUTORIALS FOR YAMMPP41RR012255 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 1997 to 2009
$10.4M
PROTEIN FOLDING THERMODYNAMICS AND KINETICSR01GM048807 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI BROOKS, CHARLES L · 1994 to 2005
$1.9M
NCRR NIH HHS P41 RR012255NCRR NIH HHS RR12255NIGMS NIH HHS GM48807NIGMS NIH HHS R01 GM048807
6 · The paper itself

Abstract

The folding of multidomain proteins often proceeds in a hierarchical fashion with individual domains folding independent of one another. A large single-domain protein, however, can consist of multiple modules whose folding may be autonomous or interdependent in ways that are unclear. We used coarse-grained simulations to explore the folding landscape of the two-subdomain bacterial response regulator CheY. Thermodynamic and kinetic characterization shows the landscape to be highly analogous to the four-state landscape reported for another two-subdomain protein, T4 lysozyme. An on-pathway intermediate structured in the more stable nucleating subdomain was observed, as were transient states frustrated in off-pathway contacts prematurely structured in the weaker subdomain. Local unfolding, or backtracking, was observed in the frustrated state before the native conformation could be reached. Nonproductive frustration was attributable to competition for van der Waals contacts between the two subdomains. In an accompanying article, stopped-flow kinetic measurements support an off-pathway burst-phase intermediate, seemingly consistent with our prediction of early frustration in the folding landscape of CheY. Comparison of the folding mechanisms for CheY, T4 lysozyme, and interleukin-1 beta leads us to postulate that subdomain competition is a general feature of large single-domain proteins with multiple folding modules.

Indexed as

Protein ConformationProtein FoldingBacterial ProteinsBacteriophage T4Computer SimulationInterleukin-1betaMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsModels, MolecularMuramidaseThermodynamicsBacterial ProteinsInterleukin-1betaMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMuramidase

Identifiers

PMID18644380
PMCPMC2564871
OpenAlexW2079171897

What OpenQuestion holds

Textmetadata
LicenceTDM
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.