ArticleProtein science : a publication of the Protein Society2022
Intrinsic protein disorder uncouples affinity from binding specificity.
Article 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 15 papers.
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Who cites it
15 citing papers in PubMed.
- Protocol for efficient purification of endotoxin-free human recombinant tau protein.STAR protocols · 2026Article
- How Binding Affinity and Binding Specificity Map to Sequence Space.Journal of molecular evolution · 2026Article
- β-catenin functions as a molecular adapter for disordered cBAF interactions.Molecular cell · 2025Article
- Assessing variant effect predictors and disease mechanisms in intrinsically disordered proteins.PLoS computational biology · 2025Article
- Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025Review
- Conformational Analyses of the AHD1-UBAN Region of TNIP1 Highlight Key Amino Acids for Interaction with Ubiquitin.Biomolecules · 2025Article
- Separation of sticker-spacer energetics governs the coalescence of metastable condensates.Biophysical journal · 2025Article
- Article
- The protein domains of vertebrate species in which selection is more effective have greater intrinsic structural disorder.bioRxiv : the preprint server for biology · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Article
- Comment on "Intrinsic protein disorder uncouples affinity from binding specificity".Protein science : a publication of the Protein Society · 2023Article
- Reply to "Intrinsic protein disorder uncouples affinity from binding specificity".Protein science : a publication of the Protein Society · 2023Article
- Article
- Intrinsic protein disorder uncouples affinity from binding specificity.Protein science : a publication of the Protein Society · 2022Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins often function by molecular recognition, in which they undergo induced folding. Based on prior generalizations, the idea prevails in the IDP field that due to the entropic penalty of induced folding, the major functional advantage associated with this binding mode is "uncoupling" specificity from binding strength. Nevertheless, both weaker binding and high specificity of IDPs/IDRs rest on limited experimental observations, making these assumptions more speculations than evidence-supported facts. The issue is also complicated by the rather vague concept of specificity that lacks an exact measure, such as the K
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Registered trials
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.