Evidence map›Paper›PMID 36948207›Full record

ArticleNano letters2023

Anisotropic Friction in a Ligand-Protein Complex.

Wanhao Cai, Miriam Jäger, Jakob T Bullerjahn, Thorsten Hugel, Steffen Wolf, Bizan N Balzer

Abstract read
In one paragraph

Article in Nano letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Highly Branched Sulfated Glycopolymers as Mucin Mimetics.Journal of the American Chemical Society · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Review
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.

Wanhao CaiInstitute of Physical Chemistry, University of Freiburg, Albertstr. 21, 79104 Freiburg, Germany.ORCID 0000-0002-3466-8530
Miriam JägerBiomolecular Dynamics, Institute of Physics, University of Freiburg, Hermann-Herder-Str. 3, 79104 Freiburg, Germany.ORCID 0000-0002-5983-5497
Jakob T BullerjahnDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Thorsten HugelInstitute of Physical Chemistry, University of Freiburg, Albertstr. 21, 79104 Freiburg, Germany.ORCID 0000-0003-3292-4569
Steffen WolfBiomolecular Dynamics, Institute of Physics, University of Freiburg, Hermann-Herder-Str. 3, 79104 Freiburg, Germany.ORCID 0000-0003-1752-6175
Bizan N BalzerInstitute of Physical Chemistry, University of Freiburg, Albertstr. 21, 79104 Freiburg, Germany.ORCID 0000-0001-6886-0857

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effect of an externally applied directional force on molecular friction is so far poorly understood. Here, we study the force-driven dissociation of the ligand-protein complex biotin-streptavidin and identify anisotropic friction as a not yet described type of molecular friction. Using AFM-based stereographic single molecule force spectroscopy and targeted molecular dynamics simulations, we find that the rupture force and friction for biotin-streptavidin vary with the pulling angle. This observation holds true for friction extracted from Kramers' rate expression and by dissipation-corrected targeted molecular dynamics simulations based on Jarzynski's identity. We rule out ligand solvation and protein-internal friction as sources of the angle-dependent friction. Instead, we observe a heterogeneity in free energy barriers along an experimentally uncontrolled orientation parameter, which increases the rupture force variance and therefore the overall friction. We anticipate that anisotropic friction needs to be accounted for in a complete understanding of friction in biomolecular dynamics and anisotropic mechanical environments.

Indexed as

BiotinMolecular Dynamics SimulationFrictionLigandsMicroscopy, Atomic ForceStreptavidinBiotinLigandsStreptavidinatomic force microscopyfrictionligand-protein complexsingle moleculesteered molecular dynamics simulationtargeted molecular dynamics simulation

Identifiers

PMID36948207
PMCPMC10214488

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.