ReviewTrends in biochemical sciences2023
Metamorphic protein folding as evolutionary adaptation.
Review in Trends in biochemical sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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Who cites it
10 citing papers in PubMed.
- Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026Article
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Fold-Switching Proteins.Annual review of biophysics · 2026Review
- Exploration of the structural and functional diversity in the metamorphic RfaH subfamily.bioRxiv : the preprint server for biology · 2026Article
- Disentangling coevolutionary constraints for modeling protein conformational heterogeneity.Communications chemistry · 2026Article
- Fold-switching proteins.ArXiv · 2025Article
- Evolving concepts of the protein universe.iScience · 2025Review
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- ColabFold predicts alternative protein structures from single sequences, coevolution unnecessary for AF-cluster.bioRxiv : the preprint server for biology · 2023Article
- Evolutionary selection of proteins with two folds.Nature communications · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Metamorphic proteins switch reversibly between multiple distinct, stable structures, often with different functions. It was previously hypothesized that metamorphic proteins arose as intermediates in the evolution of a new fold - rare and transient exceptions to the 'one sequence, one fold' paradigm. However, as described herein, mounting evidence suggests that metamorphic folding is an adaptive feature, preserved and optimized over evolutionary time as exemplified by the NusG family and the chemokine XCL1. Analysis of extant protein families and resurrected protein ancestors demonstrates that large regions of sequence space are compatible with metamorphic folding. As a category that enhances biological fitness, metamorphic proteins are likely to employ fold switching to perform important biological functions and may be more common than previously thought.
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Registered trials
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