Design and discovery of metamorphic proteins
Open accessAbstract
Metamorphic proteins are single amino acid sequences that reversibly interconvert between multiple, dramatically different native structures, often with distinct functions. Since the discovery of the first metamorphic proteins in the early 2000s, several additional metamorphic proteins have been identified, and it was suggested that up to 4% of proteins in the PDB may switch folds. Metamorphic proteins have been found to share common features such as marginal thermostability and inconsistencies in predicted secondary structures. Outstanding challenges in the field include the search for more metamorphic proteins and the design of new proteins that switch folds. Identification of novel metamorphic proteins in nature will improve therapeutic targeting of fold-switching proteins involved in human pathology and will enhance the design of protein-based therapies. Designed fold switching proteins have applications as biosensors, molecular switches, molecular machines, and self-assembling systems.
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Fewer than ten metamorphic protein families have been thoroughly experimentally characterized, spanning a diverse range of functions.
“Fewer than ten metamorphic protein families have been thoroughly experimentally characterized21, spanning a diverse range of functions.”
From Predicting multiple conformations via sequence clustering and AlphaFold2 (2024) · cites this paper as [21]
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- Authors
- Dishman, A. F., & Volkman, B. F.
- Affiliations
- Medical College of Wisconsin (US)
- Corresponding author
- Volkman, Brian F.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2022-06
- Volume
- 74
- Pages
- 102380
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC9664977
- OpenAlex
- W4229455959
- Cited by
- 36
- References
- 48
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 5 · 2023: 12 · 2022: 3
- FWCI
- 0.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Current Opinion in Structural Biology (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Funders
- National Institutes of Health (F30 CA236182, R56 AI155881, T32 GM080202)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- metamorphic proteins, fold switching, protein design, protein folding, protein-based therapy, biosensors, molecular switches
- MeSH terms
- Amino Acid Sequence, Humans, Proteins, Protein Structure, Secondary, Protein Folding
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