Sequence-dependent conformational transitions of disordered proteins during condensation.

ABSTRACT: Intrinsically disordered proteins (IDPs) can form biomolecular condensates through phase separation. It is recognized that the conformation of IDPs in the dense and dilute phases, as well as at the interfaces of condensates, can critically impact their functionality. However, a residue-level understanding of the conformational transitions of IDPs during condensation remains elusive. In this study, we employ a coarse-grained polyampholyte model, comprising an equal number of oppositely charged residues-glutamic acid and lysine-whereby conformations and phase behavior can be tuned by altering the protein sequence. By manipulating sequence patterns from perfectly alternating to block-like, we obtain chains with ideal-like conformations to semi-compact structures in the dilute phase. In the de

SUBMITTER: Wang J 

PROVIDER: S-EPMC11575531 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature