ReviewProtein science : a publication of the Protein Society2022
Simple mechanisms for the evolution of protein complexity.
Review in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Nonexpansive biodegradable matrix promotes blood vessel organoid development for neurovascular repair and functional recovery in ischaemic stroke.Nature biomedical engineering · 2026Article
- Integrating evolutionary signals and predicted protein structure reveals localized molecular divergence in Cereus lineages.Genetica · 2026Article
- Deep homology and design of proteasome chaperone proteins in Candidozyma auris.Nature communications · 2026Article
- Studying the evolutionary potential of ancestral aryl sulfatases in the alkaline phosphatase family with droplet microfluidics.The Analyst · 2026Article
- Selective control of ligand binding through a distal mutation that alters the protein native ensemble.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Directed evolution of multimeric proteins is enabled by dual-compensatory gene duplication.bioRxiv : the preprint server for biology · 2026Article
- Structural variability of multifunctional proteins indicates frequent stochastic evolution of protein oligomers.Communications biology · 2025Article
- Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape.Nature plants · 2025Article
- Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.The FEBS journal · 2025Article
- Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular and evolutionary determinants for protein interaction within a class II aldolase/Adducin domain.PloS one · 2025Article
- Symmetry facilitated the evolution of heterospecificity and high-order stoichiometry in vertebrate hemoglobin.bioRxiv : the preprint server for biology · 2024Article
- Evolutionary model of repeat insertions in Ataxin-3 traces the origin of the polyglutamine stretch to an ancestral ubiquitin binding module.Protein science : a publication of the Protein Society · 2024Article
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- Assessing the functional impact of protein binding site definition.Protein science : a publication of the Protein Society · 2024Article
- Article
- Adapting enzymes to improve their functionality in plants: why and how.Biochemical Society transactions · 2023Review
- Metamorphic protein folding as evolutionary adaptation.Trends in biochemical sciences · 2023Review
- Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection.Nature ecology & evolution · 2023Article
- Simple mechanisms for the evolution of protein complexity.Protein science : a publication of the Protein Society · 2022Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Proteins are tiny models of biological complexity: specific interactions among their many amino acids cause proteins to fold into elaborate structures, assemble with other proteins into higher-order complexes, and change their functions and structures upon binding other molecules. These complex features are classically thought to evolve via long and gradual trajectories driven by persistent natural selection. But a growing body of evidence from biochemistry, protein engineering, and molecular evolution shows that naturally occurring proteins often exist at or near the genetic edge of multimerization, allostery, and even new folds, so just one or a few mutations can trigger acquisition of these properties. These sudden transitions can occur because many of the physical properties that underlie these features are present in simpler proteins as fortuitous by-products of their architecture. Moreover, complex features of proteins can be encoded by huge arrays of sequences, so they are accessible from many different starting points via many possible paths. Because the bridges to these features are both short and numerous, random chance can join selection as a key factor in explaining the evolution of molecular complexity.
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