ArticleBiophysical journal2013
Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 0 citations in OpenAlex.
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- Interactions between Curcumin Derivatives and Amyloid-β Fibrils: Insights from Molecular Dynamics Simulations.Journal of chemical information and modeling · 2020Article
- Spontaneous self-assembly of amyloid β (1-40) into dimers.Nanoscale advances · 2019Article
- Unraveling the Thousand Word Picture: An Introduction to Super-Resolution Data Analysis.Chemical reviews · 2017Article
- Nano-assembly of amyloid β peptide: role of the hairpin fold.Scientific reports · 2017Article
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
- Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins.Journal of chemical theory and computation · 2014Article
- Recovering a representative conformational ensemble from underdetermined macromolecular structural data.Journal of the American Chemical Society · 2013Article
- Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Intrinsically disordered proteinsReview
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3 authors at 2 institutions in 1 country.
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Abstract
Quantitative comparisons of intrinsically disordered proteins (IDPs) with similar sequences, such as mutant forms of the same protein, may provide insights into IDP aggregation-a process that plays a role in several neurodegenerative disorders. Here we describe an approach for modeling IDPs with similar sequences that simplifies the comparison of the ensembles by utilizing a single library of structures. The relative population weights of the structures are estimated using a Bayesian formalism, which provides measures of uncertainty in the resulting ensembles. We applied this approach to the comparison of ensembles for Aβ40 and Aβ42. Bayesian hypothesis testing finds that although both Aβ species sample β-rich conformations in solution that may represent prefibrillar intermediates, the probability that Aβ42 samples these prefibrillar states is roughly an order of magnitude larger than the frequency in which Aβ40 samples such structures. Moreover, the structure of the soluble prefibrillar state in our ensembles is similar to the experimentally determined structure of Aβ that has been implicated as an intermediate in the aggregation pathway. Overall, our approach for comparative studies of IDPs with similar sequences provides a platform for future studies on the effect of mutations on the structure and function of disordered proteins.
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