ArticleThe journal of physical chemistry. B2026
Comparing Enhanced Sampling Methods in Exploring the Conformational Space of β-Catenin
Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Intrinsically disordered proteins (IDPs) play critical roles in cellular signaling and regulation, yet their dynamic conformational landscapes make them difficult to characterize experimentally and computationally. Phosphorylation, one of the most common post-translational modifications, frequently occurs within intrinsically disordered regions and can modulate protein structure and function. Enhanced sampling molecular dynamics methods offer a potential route to more efficiently explore the diverse conformations accessible to IDPs, but systematic comparisons of their performance sampling the conformational landscape of such systems remain limited. Here, we evaluate the conformational sampling of the intrinsically disordered β-catenin
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