Evidence map›Paper›PMID 39922965›Full record

ArticleScientific reports2025

Severe deviation in protein fold prediction by advanced AI: a case study.

Jacinto López-Sagaseta, Alejandro Urdiciain

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

2 authors.

Jacinto López-Sagaseta *Unit of Protein Crystallography and Structural Immunology, 31008, Navarrabiomed, Navarra, Spain. jacinto.lopez.sagaseta@navarra.es.
Alejandro Urdiciain *Unit of Protein Crystallography and Structural Immunology, 31008, Navarrabiomed, Navarra, Spain.

Funding

Ministerio de Ciencia e Innovación RYC-2017-21683
6 · The paper itself

Abstract

Artificial intelligence (AI) and deep learning are making groundbreaking strides in protein structure prediction. AlphaFold is remarkable in this arena for its outstanding accuracy in modelling proteins fold based solely on their amino acid sequences. In spite of these remarkable advances, experimental structure determination remains critical. Here we report severe deviations between the experimental structure of a two-domain protein and its equivalent AI-prediction. These observations are particularly relevant to the relative orientation of the domains within the global protein scaffold. We observe positional divergence in equivalent residues beyond 30 Å, and an overall RMSD of 7.7 Å. Significant deviation between experimental structures and AI-predicted models echoes the presence of unusual conformations, insufficient training data and high complexity in protein folding that can ultimately lead to current limitations in protein structure prediction.

Indexed as

Artificial IntelligenceProtein FoldingProteinsComputational BiologyDeep LearningModels, MolecularProtein ConformationProteins

Identifiers

PMID39922965
PMCPMC11807112

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.