ReviewPhysical chemistry chemical physics : PCCP2012
Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets.
Review in Physical chemistry chemical physics : PCCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Atomistic molecular dynamics simulations of intrinsically disordered proteins.Current opinion in structural biology · 2025Review
- The Magic of Proteases: From a Procoagulant and Anticoagulant Factor V to an Equitable Treatment of Its Inherited Deficiency.International journal of molecular sciences · 2023Review
- The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling.Nucleic acids research · 2022Article
- Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.Biomolecules · 2021Review
- Introducing intrinsic disorder reduces electrostatic steering in protein-protein interactions.Biophysical journal · 2021Article
- Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random.Biophysical journal · 2021Article
- Genome instability and loss of protein homeostasis: converging paths to neurodegeneration?Open biology · 2021Review
- Unraveling protein's structural dynamics: from configurational dynamics to ensemble switching guides functional mesoscale assemblies.Current opinion in structural biology · 2021Review
- Progressive Phosphorylation Modulates the Self-Association of a Variably Modified Histone H3 Peptide.Frontiers in molecular biosciences · 2021Article
- Structural basis of client specificity in mitochondrial membrane-protein chaperones.Science advances · 2020Article
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Nonclassical nuclear localization signals mediate nuclear import of CIRBP.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Intrinsically Disordered Transactivation Domains Bind to TAZ1 Domain of CBP via Diverse Mechanisms.Biophysical journal · 2019Article
- Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein.Scientific reports · 2019Article
- Position-, disorder-, and salt-dependent diffusion in binding-coupled-folding of intrinsically disordered proteins.Physical chemistry chemical physics : PCCP · 2019Article
- Extreme Fuzziness: Direct Interactions between Two IDPs.Biomolecules · 2019Review
- Molecular Mechanisms of Tight Binding through Fuzzy Interactions.Biophysical journal · 2018Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Flexibility vs Preorganization: Direct Comparison of Binding Kinetics for a Disordered Peptide and Its Exact Preorganized Analogues.The journal of physical chemistry. B · 2017Article
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3 authors.
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Abstract
The binding of intrinsically disordered proteins (IDPs) to structured targets is gaining increasing attention. Here we review experimental and computational studies on the binding kinetics of IDPs. Experiments have yielded both the binding rate constants and the binding mechanisms, the latter via mutation and deletion studies and NMR techniques. Most computational studies have aimed at qualitative understanding of the binding rate constants or at mapping the free energy surfaces after the IDPs are engaged with their targets. The experiments and computation show that IDPs generally gain structures after they are engaged with their targets; that is, interactions with the targets facilitate the IDPs' folding. It also seems clear that the initial contact of an IDP with the target is formed by just a segment, not the entire IDP. The docking of one segment to its sub-site followed by coalescing of other segments around the corresponding sub-sites emerges as a recurring feature in the binding of IDPs. Such a dock-and-coalesce model forms the basis for quantitative calculation of binding rate constants. For both disordered and ordered proteins, strong electrostatic attraction with their targets can enhance the binding rate constants by several orders of magnitude. There are now tremendous opportunities in narrowing the gap in our understanding of IDPs relative to ordered proteins with regard to binding kinetics.
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