Evidence map›Paper›PMID 37490533›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Fast protein folding is governed by memory-dependent friction.

Benjamin A Dalton, Cihan Ayaz, Henrik Kiefer, Anton Klimek, Lucas Tepper, Roland R Netz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. 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
6.6field-weighted citation impact, top 3% 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, 44 citations in OpenAlex.

  1. Hierarchical friction memory leads to subdiffusive configurational dynamics of fast-folding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Static and dynamic rough energy landscapes can lead to identical diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Nonequilibrium relaxation exponentially delays the onset of quantum diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. The Potential of Neural Network Potentials.ACS physical chemistry Au · 2024
    Review
  8. Cell migration: Beyond Brownian motion.Biophysical journal · 2024
    Article
  9. Article
  10. Accurate Memory Kernel Extraction from Discretized Time-Series Data.Journal of chemical theory and computation · 2024
    Article
  11. Article
  12. 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 at 1 institution in 1 country.

Benjamin A DaltonFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.ORCID 0000-0002-0448-2989
Cihan AyazFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.ORCID 0000-0001-7154-9744
Henrik KieferFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.ORCID 0009-0008-0841-2217
Anton KlimekFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.ORCID 0009-0008-5853-3092
Lucas TepperFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.
Roland R NetzFachbereich Physik, Freie Universität Berlin, Berlin 14195, Germany.ORCID 0000-0003-0147-0162
Freie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When described by a low-dimensional reaction coordinate, the folding rates of most proteins are determined by a subtle interplay between free-energy barriers, which separate folded and unfolded states, and friction. While it is commonplace to extract free-energy profiles from molecular trajectories, a direct evaluation of friction is far more elusive and typically relies on fits of measured reaction rates to memoryless reaction-rate theories. Here, using memory-kernel extraction methods founded on a generalized Langevin equation (GLE) formalism, we directly calculate the time-dependent friction acting on the fraction of native contacts reaction coordinate

Indexed as

Molecular Dynamics SimulationProtein FoldingFrictionProteinsProteinsgeneralized Langevin equationmolecular frictionnon-Markovian dynamicsprotein foldingreaction rate theory

Identifiers

PMID37490533
PMCPMC10401029
OpenAlexW4385236116

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.