Microphase Separation Produces Interfacial Environment within Diblock Biomolecular Condensates.

ABSTRACT: The phase separation of intrinsically disordered proteins is emerging as an important mechanism for cellular organization. However, efforts to connect protein sequences to the physical properties of condensates, i.e., the molecular grammar, are hampered by a lack of effective approaches for probing high-resolution structural details. Using a combination of multiscale simulations and fluorescence lifetime imaging microscopy experiments, we systematically explored a series of systems consisting of diblock elastin-like polypeptides (ELP). The simulations succeeded in reproducing the variation of condensate stability upon amino acid substitution and revealed different microenvironments within a single condensate, which we verified with environmentally sensitive fluorophores. The interspersion

SUBMITTER: Latham AP 

PROVIDER: S-EPMC10081284 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature