Conformational diversity and protein evolution – a 60-year-old hypothesis revisited
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There are examples of highly similar protein sequences having radically different structures and functions and of sequences that can form multiple folds.
“Although it is generally believed that proteins with similar sequences form similar structures, there are also interesting examples of highly similar protein sequences having radically different structures and functions 60,61 and of sequences that can form multiple folds 62.”
From Learning the protein language: Evolution, structure, and function (2021) · cites this paper as [62]
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The protein trinity—linking function and disorder
Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581 · see citing works
Multiple diverse ligands binding at a single protein site: A matter of pre‐existing populations
Ma, B., Shatsky, M., Wolfson, H. J., & Nussinov, R. (2002) · Protein Science · doi:10.1110/ps.21302 · Cited by 420 · see citing works
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The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008 · see citing works
Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355 · see citing works
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847 · see citing works
Enzyme promiscuity: evolutionary and mechanistic aspects
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Self-citationPrions as adaptive conduits of memory and inheritance
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Learning the protein language: Evolution, structure, and function
Bepler, T., & Berger, B. (2021) · Cell Systems · doi:10.1016/j.cels.2021.05.017 · Cited by 483 · see citing works
The role of protein dynamics in the evolution of new enzyme function
Campbell, E., Kaltenbach, M., Correy, G. J., Carr, P. D., Porebski, B. T., Livingstone, E. K., Afriat-Jurnou, L., Buckle, A. M., Weik, M., Hollfelder, F., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2175 · Cited by 311 · see citing works
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Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics
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Protein structure prediction by <i>AlphaFold</i> 2: are attention and symmetries all you need?
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- Authors
- James, L. C., & Tawfik, D. S.
- Affiliations
- University of Cambridge (GB)
- Weizmann Institute of Science (IL)
- Corresponding author
- Tawfik, Dan S.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 28
- Issue
- 7
- Pages
- 361-368
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2106531843
- Cited by
- 579
- References
- 2
- Citations by year
- 2026: 13 · 2025: 24 · 2024: 24 · 2023: 22 · 2022: 31 · 2021: 27 · 2020: 26 · 2019: 26 · 2018: 22 · 2017: 24 · 2016: 19 · 2015: 30 · 2014: 17 · 2013: 34 · 2012: 32
- FWCI
- 1.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Israel Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- conformational heterogeneity, protein evolution, protein folding, protein function, sequence-structure-function relationships, protein origin, functional diversity
- MeSH terms
- Animals, Humans, Protein Conformation, Proteins, Evolution, Molecular
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