ArticleBiophysical journal2012
Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Refining the pool of RNA-binding domains advances the classification and prediction of RNA-binding proteins.Nucleic acids research · 2024Article
- Combined prediction and design reveals the target recognition mechanism of an intrinsically disordered protein interaction domain.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Understanding protein diffusion on force-induced stretched DNA conformation.Frontiers in molecular biosciences · 2022Article
- Effects of Topology and Sequence in Protein Folding Linked via Conformational Fluctuations.Biophysical journal · 2020Article
- Modulation of the aggregation of an amyloidogenic sequence by flanking-disordered region in the intrinsically disordered antigen merozoite surface protein 2.European biophysics journal : EBJ · 2019Article
- Subunit Interactions within the Carbon-Phosphorus Lyase Complex from Escherichia coli.Biochemistry · 2015Article
- Knotted proteins: A tangled tale of Structural Biology.Computational and structural biotechnology journal · 2015Review
- Smooth functional transition along a mutational pathway with an abrupt protein fold switch.Biophysical journal · 2014Article
- Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Inherent relationships among different biophysical prediction methods for intrinsically disordered proteins.Biophysical journal · 2013Article
- Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.PLoS computational biology · 2013Article
- Effects of knots on protein folding properties.PloS one · 2013Article
- Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Biophysical journal · 2012Article
- How difficult is it to fold a knotted protein? In silico insights from surface-tethered folding experiments.PloS one · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coupled folding-binding is central to the function of many intrinsically disordered proteins, yet not fully understood. With a continuous three-letter protein model, we explore the free-energy landscape of pairs of interacting sequences and how it is impacted by 1), variations in the binding mechanism; and 2), the addition of disordered flanks to the binding region. In particular, we focus on two sequences, one with 16 and one with 35 amino acids, which make a stable dimeric three-helix bundle at low temperatures. Three distinct binding mechanisms are realized by altering the stabilities of the individual monomers: docking, coupled folding-binding of a single α-helix, and synergistic folding and binding. Compared to docking, the free-energy barrier for binding is reduced when the single α-helix is allowed to fold upon binding, but only marginally. A greater reduction is found for synergistic folding, which in addition results in a binding transition state characterized by very few interchain contacts. Disordered flanking chain segments attached to the α-helix sequence can, despite a negligible impact on the dimer stability, lead to a downhill free-energy surface in which the barrier for binding is eliminated.
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