Evidence map›Paper›PMID 33765390›Full record

ArticleNano letters2021

Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.

Andrew Stannard, Marc Mora, Amy E M Beedle, Marta Castro-López, Stephanie Board, Sergi Garcia-Manyes

Open access · greenAbstract read
In one paragraph

Article in Nano letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. A Hierarchical Mechanotransduction System: From Macro to Micro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. 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 1 institution in 1 country.

Andrew StannardDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.ORCID 0000-0001-6283-667X
Marc MoraDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.
Amy E M BeedleDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.
Marta Castro-LópezDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.
Stephanie BoardDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.
Sergi Garcia-ManyesDepartment of Physics, Randall Centre for Cell and Molecular Biophysics and London Centre for Nanotechnology, King's College London, Strand, WC2R 2LS London, United Kingdom.ORCID 0000-0001-5140-2606
King's College London · GB

Funding

Cancer Research UK FC001002Wellcome Trust 210887Wellcome Trust 210887/Z/18/ZWellcome Trust 212218/Z/18/ZWellcome Trust FC001002
6 · The paper itself

Abstract

Molecular fluctuations directly reflect the underlying energy landscape. Variance analysis examines protein dynamics in several biochemistry-driven approaches, yet measurement of probe-independent fluctuations in proteins exposed to mechanical forces remains only accessible through steered molecular dynamics simulations. Using single molecule magnetic tweezers, here we conduct variance analysis to show that individual unfolding and refolding transitions occurring in dynamic equilibrium in a single protein under force are hallmarked by a change in the protein's end-to-end fluctuations, revealing a change in protein stiffness. By unfolding and refolding three structurally distinct proteins under a wide range of constant forces, we demonstrate that the associated change in protein compliance to reach force-induced thermodynamically stable states scales with the protein's contour length increment, in agreement with the sequence-independent freely jointed chain model of polymer physics. Our findings will help elucidate the conformational dynamics of proteins exposed to mechanical force at high resolution which are of central importance in mechanosensing and mechanotransduction.

Indexed as

Mechanotransduction, CellularProtein FoldingMechanical PhenomenaProtein ConformationProteinsProteinsenergy landscapeprotein fluctuationsprotein foldingprotein nanomechanicsprotein stiffnesssingle molecule magnetic tweezers

Identifiers

PMID33765390
PMCPMC7610714
OpenAlexW3136814143

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.