Evidence map›Paper›PMID 25796331›Full record

ArticleBiochemical and biophysical research communications2015

The elastic free energy of a tandem modular protein under force.

Jessica Valle-Orero, Edward C Eckels, Guillaume Stirnemann, Ionel Popa, Ronen Berkovich, Julio M Fernandez

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. A PDZ tandem repeat folds and unfolds via different pathways.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
  4. Review
  5. Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Mechanical Deformation Accelerates Protein Ageing.Angewandte Chemie (International ed. in English) · 2017
    Article
  13. Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017
    Article
  14. Multidomain proteins under force.Nanotechnology · 2017
    Article
  15. A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016
    Article
  16. 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

6 authors at 3 institutions in 3 countries.

Jessica Valle-OreroDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. Electronic address: jv2499@columbia.edu.
Edward C EckelsDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Guillaume StirnemannLaboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, 13, rue Pierre et Marie Curie, 75005 Paris, France.
Ionel PopaDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Ronen BerkovichDepartment of Chemical Engineering, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Julio M FernandezDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. Electronic address: jfernandez@columbia.edu.
Columbia University · USBen-Gurion University of the Negev · ILSorbonne Université · FR

Funding

Single Molecule Studies of Titin ElasticityR01HL061228 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI FERNANDEZ, JULIO M · 1999 to 2017
$7.4M
Nanomechanics of the extracellular matrixR01HL066030 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI FERNANDEZ, JULIO M · 2001 to 2013
$5.0M
NHLBI NIH HHS HL61228NHLBI NIH HHS HL66030NHLBI NIH HHS R01 HL061228NHLBI NIH HHS R01 HL066030
6 · The paper itself

Abstract

Recent studies have provided a theoretical framework for including entropic elasticity in the free energy landscape of proteins under mechanical force. Accounting for entropic elasticity using polymer physics models has helped explain the hopping behavior seen in single molecule experiments in the low force regime. Here, we expand on the construction of the free energy of a single protein domain under force proposed by Berkovich et al. to provide a free energy landscape for N tandem domains along a continuous polypeptide. Calculation of the free energy of individual domains followed by their concatenation provides a continuous free energy landscape whose curvature is dominated by the worm-like chain at forces below 20 pN. We have validated our free energy model using Brownian dynamics and reproduce key features of protein folding. This free energy model can predict the effects of changes in the elastic properties of a multidomain protein as a consequence of biological modifications such as phosphorylation or the formation of disulfide bonds. This work lays the foundations for the modeling of tissue elasticity, which is largely determined by the properties of tandem polyproteins.

Indexed as

ElasticityProteinsProteinsForce spectroscopyFree energy landscapeLangevin dynamicsProtein foldingTandem modular proteinTissue elasticity

Identifiers

PMID25796331
PMCPMC4445072
OpenAlexW2020146839

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.