Capturing nested information from disordered peptide phases

Anfinsen's dogma emerged from experiments which show that a protein's native 3D folded architecture is encoded within its primary sequence. This insight emerged before almost 40% of eukaryotic proteins were found to contain intrinsically disordered domains with binding partners that are able to template multiple structures and functional outputs. Despite the challenges associated with characterizing such intrinsically disordered protein domains and their interactions with various binding partners, the need to understand how they propagate and regulate context‐dependent information now becomes increasingly important. In addition to understanding the complex signaling networks of multicellular organisms, harness their potential will expand the next generation of functional materials. Accordingly, we review progress with model peptides to reveal the rules necessary for precise spatiotemporal assembly of polypeptide materials.