ArticleProceedings of the National Academy of Sciences of the United States of America2011
On the role of frustration in the energy landscapes of allosteric proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
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Who cites it
109 citing papers in PubMed.
- Trans-interface coupling in the tetrameric enzyme underlies allosteric control inJournal of structural biology: X · 2026Article
- From static structures to dynamic energy landscapes: the latest revolution in molecular biology.Current opinion in structural biology · 2026Review
- A dynamically frustrated allosteric checkpoint consistent with conformational proofreading in CRISPR-Cas9.Nucleic acids research · 2026Article
- Interpreting human genetic variation at atomic resolution.Nature genetics · 2026Review
- Redesign of energetically frustrated regions rescues function in defective T4 clamp loaders.Molecular biology and evolution · 2026Article
- Protein Surface Site Determines the Evolutionary Accessibility of Allosteric Regulation.bioRxiv : the preprint server for biology · 2026Article
- A geometric criterion links HIV-1 capsid topography to its biophysical properties and function.Nature communications · 2026Article
- Advances and challenges in multiscale biomolecular simulations: artificial intelligence-driven paradigm shift.Quantitative biology (Beijing, China) · 2026Article
- Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026Review
- Probing the dark energy in the functional protein universe.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dissecting the Structural Features of Folding Asymmetry and Transient Misfolding in a Multidomain PDZ Scaffold.Small science · 2026Article
- Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025Article
- Sequence-based calculation of local energetic frustration in proteins.Structural dynamics (Melville, N.Y.) · 2025Article
- Role of frustrations in cell reprogramming.PNAS nexus · 2025Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- The AD3 locus of synaptotagmin-1 C2 domains modulates domain stability.Biophysical journal · 2025Article
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins.Biology direct · 2025Article
- Hidden high-risk states identification from routine urban traffic.PNAS nexus · 2025Article
- Advancing Deep Variant Phenotyping of Mitochondrial Enzyme Complexes For Precision Medicine in Allogeneic Hematopoietic Stem-Cell Transplantation.Transplantation reports · 2025Article
49 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Natural protein domains must be sufficiently stable to fold but often need to be locally unstable to function. Overall, strong energetic conflicts are minimized in native states satisfying the principle of minimal frustration. Local violations of this principle open up possibilities to form the complex multifunnel energy landscapes needed for large-scale conformational changes. We survey the local frustration patterns of allosteric domains and show that the regions that reconfigure are often enriched in patches of highly frustrated interactions, consistent both with the idea that these locally frustrated regions may act as specific hinges or that proteins may "crack" in these locations. On the other hand, the symmetry of multimeric protein assemblies allows near degeneracy by reconfiguring while maintaining minimally frustrated interactions. We also anecdotally examine some specific examples of complex conformational changes and speculate on the role of frustration in the kinetics of allosteric change.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.