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 the resulting properties associated with their functionality. However, a comprehensive 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 readily tuned by altering the protein sequence. By manipulating the sequence patterns from perfectly alternating to block-like, we obtain chains with ideal-like conformations to sem

SUBMITTER: Wang J 

PROVIDER: S-EPMC10802556 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature