Conformational fluidity of intrinsically disordered proteins in crowded environment: a molecular dynamics simulation study.

ABSTRACT: The class of intrinsically disordered proteins lacks stable three-dimensional structures. Their flexibility allows them to engage in a wide variety of interactions with other biomolecules thus making them biologically relevant and efficient. The intrinsic disorders of these proteins, which undergo binding-induced folding, allow alterations in their topologies while conserving their binding sites. Due to the lack of well-defined three-dimensional structures in the absence of their physiological partners, the folding and the conformational dynamics of these proteins remained poorly understood. Particularly, it is unclear how these proteins exist in the crowded intracellular milieu. In the present study, molecular dynamic simulations of two intrinsically unstructured proteins and two controls

SUBMITTER: Shult C 

PROVIDER: S-EPMC11910382 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature