ArticleProceedings of the National Academy of Sciences of the United States of America2025
Unveiling the cold reality of metamorphic proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. 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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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.
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Who cites it
10 citing papers in PubMed.
- From static structures to dynamic energy landscapes: the latest revolution in molecular biology.Current opinion in structural biology · 2026Review
- Review
- Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026Article
- Fold-Switching Proteins.Annual review of biophysics · 2026Review
- Effects of sodium chloride on circadian period and temperature compensation of KaiC phosphorylation.Scientific reports · 2026Article
- Article
- Proteome-wide identification of metamorphic protein candidates using mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Large protein databases reveal structural complementarity and functional locality.Nature communications · 2025Article
- Fold-switching proteins.ArXiv · 2025Article
- The cyanobacterial circadian clock.Npj biological timing and sleep · 2025Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Metamorphic proteins switch reversibly between two differently folded states under a variety of environmental conditions. Their identification and prediction are gaining attention, but the fundamental physicochemical basis for fold switching remains poorly understood. In this Perspective article, we address this problem by surveying the landscape of well-characterized metamorphic proteins and noting that a significant fraction of them display temperature sensitivity. We then make the case that the dependence on temperature, in particular cold-denaturation effects, is likely to be an underlying property of many metamorphic proteins regardless of their ultimate triggering mechanisms, especially those with a single domain. The argument is supported by rigorous analysis of hydrophobic effects in each well-characterized metamorphic protein pair and a description of how these parameters relate to temperature. The conclusion discusses the relevance of these insights to a better understanding of prediction, evolution, and de novo design strategies for metamorphic proteins.
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Registered trials
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