ArticlePLoS biology2014
Protein flexibility facilitates quaternary structure assembly and evolution.
Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 107 citations in OpenAlex.
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- Dynamic energy conversion in protein catalysis: From brownian motion to enzymatic function.Computational and structural biotechnology journal · 2025Review
- Evolution of Intrinsic Disorder in Protein Loops.Life (Basel, Switzerland) · 2023Article
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- The Statistical Trends of Protein Evolution: A Lesson from AlphaFold Database.Molecular biology and evolution · 2022Article
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- Rethinking the MtInhA tertiary and quaternary structure flexibility: a molecular dynamics view.Journal of molecular modeling · 2022Article
- Unravelling the molecular interactions between the SARS-CoV-2 RBD spike protein and various specific monoclonal antibodies.Biochimie · 2022Article
- IgG1-b12-HIV-gp120 Interface in Solution: A Computational Study.Journal of chemical information and modeling · 2022Article
- Menzerath-Altmann's Law of Syntax in RNA Accretion History.Life (Basel, Switzerland) · 2021Article
- Determining the interaction status and evolutionary fate of duplicated homomeric proteins.PLoS computational biology · 2020Article
- Electrochemical Characterization of a Complex FeFe Hydrogenase, the Electron-Bifurcating Hnd FromFrontiers in chemistry · 2020Article
- The importance of the quaternary structure to represent conformational ensembles of the major Mycobacterium tuberculosis drug target.Scientific reports · 2019Article
- Evolution of protein interfaces in multimers and fibrils.The Journal of chemical physics · 2019Article
- Emergence of Hierarchical Modularity in Evolving Networks Uncovered by Phylogenomic Analysis.Evolutionary bioinformatics online · 2019Review
- Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 fromMicroorganisms · 2018Article
- Ligand Binding Site Structure Influences the Evolution of Protein Complex Function and Topology.Cell reports · 2018Article
- Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.Nature structural & molecular biology · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The intrinsic flexibility of proteins allows them to undergo large conformational fluctuations in solution or upon interaction with other molecules. Proteins also commonly assemble into complexes with diverse quaternary structure arrangements. Here we investigate how the flexibility of individual protein chains influences the assembly and evolution of protein complexes. We find that flexibility appears to be particularly conducive to the formation of heterologous (i.e., asymmetric) intersubunit interfaces. This leads to a strong association between subunit flexibility and homomeric complexes with cyclic and asymmetric quaternary structure topologies. Similarly, we also observe that the more nonhomologous subunits that assemble together within a complex, the more flexible those subunits tend to be. Importantly, these findings suggest that subunit flexibility should be closely related to the evolutionary history of a complex. We confirm this by showing that evolutionarily more recent subunits are generally more flexible than evolutionarily older subunits. Finally, we investigate the very different explorations of quaternary structure space that have occurred in different evolutionary lineages. In particular, the increased flexibility of eukaryotic proteins appears to enable the assembly of heteromeric complexes with more unique components.
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