Energy Landscapes and Structural Plasticity of Intrinsically Disordered Histones.

ABSTRACT: Intrinsically disordered proteins (IDPs) are characterized by their lack of a stable 3D structure, enabling them to adopt multiple conformations and participate in various cellular processes. This study investigates the conformational dynamics of histone tails, specifically the H4 tail and the linker histone H1, focusing on the effects of post-translational modifications (PTMs) such as acetylation. Utilizing the energy landscape visualization method (ELViM), we projected the conformational space of wild type and acetylated forms of the H4 tail, revealing significant insights into their structural heterogeneity and preferential ensembles. This approach demonstrated that acetylation reduces the conformational heterogeneity of the H4 tail and introduces regions within the conformational space

SUBMITTER: Viegas RG 

PROVIDER: S-EPMC12381848 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature