Evidence map›Paper›PMID 39673466›Full record

ArticleProtein science : a publication of the Protein Society2025

Predicting absolute protein folding stability using generative models.

Matteo Cagiada, Sergey Ovchinnikov, Kresten Lindorff-Larsen

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. ANYI: The ANnotated Yeast Interactome.bioRxiv : the preprint server for biology · 2026
    Article
  5. Supervised learning of protein variant effects across large-scale mutagenesis datasets.Protein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Prediction of phase-separation propensities of disordered proteins from sequence.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Protein stability models fail to capture epistatic interactions of double point mutations.Protein science : a publication of the Protein Society · 2025
    Article
  20. Predicting absolute protein folding stability using generative models.Protein science : a publication of the Protein Society · 2025
    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

3 authors.

Matteo CagiadaLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Sergey OvchinnikovDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Kresten Lindorff-LarsenLinderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4750-6039

Funding

Carlsberg Foundation CF21-0392Novo Nordisk Foundation NNF18OC0033950
6 · The paper itself

Abstract

While there has been substantial progress in our ability to predict changes in protein stability due to amino acid substitutions, progress has been slower in methods to predict the absolute stability of a protein. Here, we show how a generative model for protein sequence can be leveraged to predict absolute protein stability. We benchmark our predictions across a broad set of proteins and find a mean error of 1.5 kcal/mol and a correlation coefficient of 0.7 for the absolute stability across a range of natural, small- to medium-sized proteins up to ca. 150 amino acid residues. We analyze current limitations and future directions including how such a model may be useful for predicting conformational free energies. Our approach is simple to use and freely available at an online implementation available via https://github.com/KULL-Centre/_2024_cagiada_stability.

Indexed as

Protein FoldingProteinsProtein StabilityModels, MolecularProtein ConformationThermodynamicsProteinsmachine learningprotein foldingprotein stabilitythermodynamics

Identifiers

PMID39673466
PMCPMC11645669

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.