Evidence map›Paper›PMID 34224747›Full record

ReviewJournal of molecular biology2021

The Protein Folding Problem: The Role of Theory.

Roy Nassar, Gregory L Dignon, Rostam M Razban, Ken A Dill

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Review
  8. Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Protein folding: Funnel model revised.Computational and structural biotechnology journal · 2024
    Article
  15. Article
  16. Article
  17. Origins of Life: The Protein Folding Problem all over again?Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  19. Article
  20. 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

4 authors.

Roy NassarLaufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA; Department of Chemistry, Stony Brook University, Stony Brook, NY, USA.
Gregory L DignonLaufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA.
Rostam M RazbanLaufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA.
Ken A DillLaufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA; Department of Chemistry, Stony Brook University, Stony Brook, NY, USA; Department of Physics and Astronomy, Stony Brook University, Stony Brook, NY, USA. Electronic address: dill@laufercenter.org.

Funding

Solvation modeling for next-gen biomolecule simulationsRM1GM135136 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI COUTSIAS, EVANGELOS A., DILL, KEN A · 2020 to 2024
$6.0M
NIGMS NIH HHS RM1 GM135136
6 · The paper itself

Abstract

The protein folding problem was first articulated as question of how order arose from disorder in proteins: How did the various native structures of proteins arise from interatomic driving forces encoded within their amino acid sequences, and how did they fold so fast? These matters have now been largely resolved by theory and statistical mechanics combined with experiments. There are general principles. Chain randomness is overcome by solvation-based codes. And in the needle-in-a-haystack metaphor, native states are found efficiently because protein haystacks (conformational ensembles) are funnel-shaped. Order-disorder theory has now grown to encompass a large swath of protein physical science across biology.

Indexed as

Protein FoldingAnimalsHumansIntrinsically Disordered ProteinsModels, MolecularProtein AggregatesProtein ConformationProteinsIntrinsically Disordered ProteinsProtein AggregatesProteinscoarse-grained modelingdisordered proteinsprotein aggregationprotein folding theorystatistical mechanics

Identifiers

PMID34224747
PMCPMC8547331

What OpenQuestion holds

Textmetadata
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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.