ArticlePloS one2010
Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteins.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Explicit Characterization of the Free Energy Landscape of pKID-KIX Coupled Folding and Binding.ACS central science · 2019Article
- Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance.Nature reviews. Cancer · 2018Review
- pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Biophysical journal · 2017Article
- Flexibility vs Preorganization: Direct Comparison of Binding Kinetics for a Disordered Peptide and Its Exact Preorganized Analogues.The journal of physical chemistry. B · 2017Article
- Dimensions, energetics, and denaturant effects of the protein unstructured state.Protein science : a publication of the Protein Society · 2016Article
- Specificity and affinity quantification of flexible recognition from underlying energy landscape topography.PLoS computational biology · 2014Article
- Advantages of proteins being disordered.Protein science : a publication of the Protein Society · 2014Review
- 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
- Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.PLoS computational biology · 2013Article
- Electrostatically accelerated encounter and folding for facile recognition of intrinsically disordered proteins.PLoS computational biology · 2013Article
- Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins.Journal of molecular biology · 2012Article
- Article
- Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks.Biophysical journal · 2012Article
- Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics study.PLoS computational biology · 2012Article
- Expanding the proteome: disordered and alternatively folded proteins.Quarterly reviews of biophysics · 2011Article
- Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 protein.International journal of molecular sciences · 2011Article
- Insights into the Binding of Intrinsically Disordered Proteins from Molecular Dynamics Simulation.Wiley interdisciplinary reviews. Computational molecular scienceArticle
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2 authors.
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Abstract
Proteins function by interacting with other molecules, where both native and nonnative interactions play important roles. Native interactions contribute to the stability and specificity of a complex, whereas nonnative interactions mainly perturb the binding kinetics. For intrinsically disordered proteins (IDPs), which do not adopt rigid structures when being free in solution, the role of nonnative interactions may be more prominent in binding processes due to their high flexibilities. In this work, we investigated the effect of nonnative hydrophobic interactions on the coupled folding and binding processes of IDPs and its interplay with chain flexibility by conducting molecular dynamics simulations. Our results showed that the free-energy profiles became rugged, and intermediate states occurred when nonnative hydrophobic interactions were introduced. The binding rate was initially accelerated and subsequently dramatically decreased as the strength of the nonnative hydrophobic interactions increased. Both thermodynamic and kinetic analysis showed that disordered systems were more readily affected by nonnative interactions than ordered systems. Furthermore, it was demonstrated that the kinetic advantage of IDPs ("fly-casting" mechanism) was enhanced by nonnative hydrophobic interactions. The relationship between chain flexibility and protein aggregation is also discussed.
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