Evidence map›Paper›PMID 16542678›Full record

ArticleJournal of molecular biology2006

Elucidating quantitative stability/flexibility relationships within thioredoxin and its fragments using a distance constraint model.

Donald J Jacobs, Dennis R Livesay, Jeremy Hules, Maria Luisa Tasayco

Abstract read
In one paragraph

Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Article
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  8. Ensemble properties of network rigidity reveal allosteric mechanisms.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
  9. Article
  10. Article
  11. Characterizing protein motions from structure.Journal of molecular graphics & modelling · 2011
    Article
  12. Article
  13. Article
  14. Ensemble-based methods for describing protein dynamics.Current opinion in pharmacology · 2010
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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.

Donald J JacobsDepartment of Physics and Optical Science, University of North Carolina, Charlotte, 9201 University City Blvd, Charlotte, NC 28227, USA. djacobs1@email.uncc.edu
Dennis R Livesay
Jeremy Hules
Maria Luisa Tasayco

Funding

TRANSITION TO ADULTHOOD OF PHYSICALLY CHALLENGED YOUTHS06GM048680 · NIGMS · CALIFORNIA STATE UNIVERSITY NORTHRIDGE · PI DE BELLARD, MARIA ELENA · 1993 to 2009
$14.0M
NIGMS NIH HHS S06 GM048680NIGMS NIH HHS S06 GM48680-0952
6 · The paper itself

Abstract

Numerous quantitative stability/flexibility relationships, within Escherichia coli thioredoxin (Trx) and its fragments are determined using a minimal distance constraint model (DCM). A one-dimensional free energy landscape as a function of global flexibility reveals Trx to fold in a low-barrier two-state process, with a voluminous transition state. Near the folding transition temperature, the native free energy basin is markedly skewed to allow partial unfolded forms. Under native conditions the skewed shape is lost, and the protein forms a compact structure with some flexibility. Predictions on ten Trx fragments are generally consistent with experimental observations that they are disordered, and that complementary fragments reconstitute. A hierarchical unfolding pathway is uncovered using an exhaustive computational procedure of breaking interfacial cross-linking hydrogen bonds that span over a series of fragment dissociations. The unfolding pathway leads to a stable core structure (residues 22-90), predicted to act as a kinetic trap. Direct connection between degree of rigidity within molecular structure and non-additivity of free energy is demonstrated using a thermodynamic cycle involving fragments and their hierarchical unfolding pathway. Additionally, the model provides insight about molecular cooperativity within Trx in its native state, and about intermediate states populating the folding/unfolding pathways. Native state cooperativity correlation plots highlight several flexibly correlated regions, giving insight into the catalytic mechanism that facilitates access to the active site disulfide bond. Residual native cooperativity correlations are present in the core substructure, suggesting that Trx can function when it is partly unfolded. This natively disordered kinetic trap, interpreted as a molten globule, has a wide temperature range of metastability, and it is identified as the "slow intermediate state" observed in kinetic experiments. These computational results are found to be in overall agreement with a large array of experimental data.

Indexed as

Models, BiologicalComputer SimulationEscherichia coliModels, MolecularPeptide FragmentsPliabilityProtein DenaturationProtein FoldingProtein Structure, TertiaryTemperatureThermodynamicsThioredoxinsPeptide FragmentsThioredoxins

Identifiers

PMID16542678
PMCPMC4667950

What OpenQuestion holds

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Registered trials

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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.