ArticleBiophysical journal2012
Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription.Oncogenesis · 2024Article
- Driving forces of the complex formation between highly charged disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
- Intrinsic protein disorder uncouples affinity from binding specificity.Protein science : a publication of the Protein Society · 2022Article
- On the role of phase separation in the biogenesis of membraneless compartments.The EMBO journal · 2022Article
- Full structural ensembles of intrinsically disordered proteins from unbiased molecular dynamics simulations.Communications biology · 2021Article
- Two Differential Binding Mechanisms of FG-Nucleoporins and Nuclear Transport Receptors.Cell reports · 2018Article
- Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Finding Our Way in the Dark Proteome.Journal of the American Chemical Society · 2016Article
- Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.The Journal of biological chemistry · 2016Review
- Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling.Journal of molecular biology · 2015Article
- Globular and disordered-the non-identical twins in protein-protein interactions.Frontiers in molecular biosciences · 2015Article
- Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.The Journal of chemical physics · 2014Article
- A frustrated binding interface for intrinsically disordered proteins.The Journal of biological chemistry · 2014Article
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.The journal of physical chemistry. B · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Many intrinsically disordered proteins (IDPs) are significantly unstructured under physiological conditions. A number of these IDPs have been shown to undergo coupled folding and binding reactions whereby they can gain structure upon association with an appropriate partner protein. In general, these systems display weaker binding affinities than do systems with association between completely structured domains, with micromolar K(d) values appearing typical. One such system is the association between α- and β-spectrin, where two partially structured, incomplete domains associate to form a fully structured, three-helix bundle, the spectrin tetramerization domain. Here, we use this model system to demonstrate a method for fitting association and dissociation kinetic traces where, using typical biophysical concentrations, the association reactions are expected to be highly reversible. We elucidate the unusually slow, two-state kinetics of spectrin assembly in solution. The advantages of studying kinetics in this regime include the potential for gaining equilibrium constants as well as rate constants, and for performing experiments with low protein concentrations. We suggest that this approach would be particularly appropriate for high-throughput mutational analysis of two-state reversible binding processes.
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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.