Evidence map›Paper›PMID 38056002›Full record

ArticleThe journal of physical chemistry letters2023

Liquid-Liquid Phase Separation of the Intrinsically Disordered Domain of the Fused in Sarcoma Protein Results in Substantial Slowing of Hydration Dynamics.

Carola S Krevert, Daniel Chavez, Sayantan Chatterjee, Lukas S Stelzl, Sabine Pütz, Steven J Roeters, Joseph F Rudzinski, Nicolas L Fawzi, Martin Girard, Sapun H Parekh and 1 more

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. All-atom simulations of biomolecular condensates.Current opinion in structural biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Deciphering Spectroscopic Signatures of Competing CaThe journal of physical chemistry. B · 2024
    Article
  14. 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

11 authors.

Carola S KrevertDepartment of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
Daniel ChavezDepartment of Polymer Theory, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
Sayantan ChatterjeeDepartment of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
Lukas S StelzlKOMET 1, Institute of Physics, Johannes Gutenberg University, Staudingerweg 7, 55099 Mainz, Germany.ORCID 0000-0002-5348-0277
Sabine PützDepartment of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
Steven J RoetersDepartment of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.ORCID 0000-0003-3238-2181
Joseph F RudzinskiDepartment of Polymer Theory, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.ORCID 0000-0003-3403-640X
Nicolas L FawziDepartment of Molecular Biology, Cell Biology, and Biochemistry, Brown University, 70 Ship Street, Providence, Rhode Island 02912, United States.ORCID 0000-0001-5483-0577
Martin GirardDepartment of Polymer Theory, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.ORCID 0000-0003-2051-6218
Sapun H ParekhDepartment of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.ORCID 0000-0001-8522-1854
Johannes HungerDepartment of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.ORCID 0000-0002-4419-5220

Funding

Residue-by-residue details of FUS protein phase separation and aggregationR01GM147677 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2022 to 2025
$1.7M
NIGMS NIH HHS R01 GM147677
6 · The paper itself

Abstract

Formation of liquid condensates plays a critical role in biology via localization of different components or via altered hydrodynamic transport, yet the hydrogen-bonding environment within condensates, pivotal for solvation, has remained elusive. We explore the hydrogen-bond dynamics within condensates formed by the low-complexity domain of the fused in sarcoma protein. Probing the hydrogen-bond dynamics sensed by condensate proteins using two-dimensional infrared spectroscopy of the protein amide I vibrations, we find that frequency-frequency correlations of the amide I vibration decay on a picosecond time scale. Interestingly, these dynamics are markedly slower for proteins in the condensate than in a homogeneous protein solution, indicative of different hydration dynamics. All-atom molecular dynamics simulations confirm that lifetimes of hydrogen-bonds between water and the protein are longer in the condensates than in the protein in solution. Altered hydrogen-bonding dynamics may contribute to unique solvation and reaction dynamics in such condensates.

Indexed as

SarcomaAmidesHumansHydrogenProteinsAmidesHydrogenProteins

Identifiers

PMID38056002
PMCPMC10726384

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.