Evidence map›Paper›PMID 39801626›Full record

ArticleArXiv2024

Proteins with alternative folds reveal blind spots in AlphaFold-based protein structure prediction.

Devlina Chakravarty, Myeongsang Lee, Lauren L Porter

Abstract readPreprint
PubMed Full text at PMC
In one paragraph

Article in ArXiv, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Devlina ChakravartyNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894.
Myeongsang LeeNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894.
Lauren L PorterNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, advances in artificial intelligence (AI) have transformed structural biology, particularly protein structure prediction. Though AI-based methods, such as AlphaFold (AF), often predict single conformations of proteins with high accuracy and confidence, predictions of alternative folds are often inaccurate, low-confidence, or simply not predicted at all. Here, we review three blind spots that alternative conformations reveal about AF-based protein structure prediction. First, proteins that assume conformations distinct from their training-set homologs can be mispredicted. Second, AF overrelies on its training set to predict alternative conformations. Third, degeneracies in pairwise representations can lead to high-confidence predictions inconsistent with experiment. These weaknesses suggest approaches to predict alternative folds more reliably.

Indexed as

Alternative conformationsDeep LearningFold-switching proteinsMachine Learningmetamorphic proteinsprotein structure prediction

Identifiers

PMID39801626
PMCPMC11722503

What OpenQuestion holds

Textmetadata
LicenceCC0
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.