Linking disordered protein sequence and ensemble using interaction maps

Abstract

Intrinsically disordered protein regions (IDRs) do not have a stable native structure and instead exist in a constantly changing conformational ensemble that can determine their function. While global or average sequence features such as charge or aromatic residue distribution can sometimes predict the structure of IDR ensembles, a complete understanding of how the structure is encoded in IDR sequences remains elusive. We posit that this information is encoded in the intramolecular interactions of these sequences.