MCB Joint Seminar Series: Wenwei Zheng

Intrinsically disordered proteins (IDPs) lack stable three-dimensional folds yet play essential roles in the cell, with function encoded in conformational ensembles rather than single structures. In this talk, I will describe how sequence-encoded interactions organize IDP ensembles at three levels: global features that govern liquid–liquid phase separation, local transient interactions that regulate transcriptional activity, and topological entanglement that links ensemble organization to biological function across the human disordered proteome. These studies suggest that disorder at the monomeric level can be highly organized at the ensemble level.