The question of how the primary sequence of a protein determines its three-dimensional structure remains unanswered. One approach is to make de-novo designs of peptides and proteins that should adopt a predetermined secondary and tertiary structure. Our lab seeks to design synthetic helical peptide filaments, taking inspiration from filamentous protein assemblies that abundantly occur in nature. Helical protein assemblies found naturally, for example, actin and tubulin homologues, flagellin, and pili encompass various functionalities that are desirable to emulate in synthetic systems for applications including controlled release and delivery, cargo transport, locomotion, energy transduction, and signal transduction. However, it remains challenging to achieve the level of structural control seen in native biological assemblies for synthetic assemblies. At the Conticello lab, we create analogues of biologically derived protein filaments to understand the sequence-structure relationship that underlies the self-assembly process and try to decipher the structural clues necessary for the de-novo design of helical polymer. The insights obtained will guide reliable structural prediction and sequence design of self-assembling peptides.