A protein’s three-dimensional structure is crucial for its biological function.Exploring of how the protein sequence and posttranslational modificationsdetermine the structure is fundamental to an improved understanding of themechanisms of protein folding and misfolding. Beyond that, this knowledge canbe used to design new peptides and proteins with novel structures and functions.The research of the Thomas group is centered around this key problem. We usede novo designed peptide building blocks to create biomimetic systems. Thisincludes firstly, the uncovering of the sequence-to-structure relationships; and,secondly, engineering of the scaffold to modulate function. We focus on smallwell-characterized self-assembling and reliably folding peptides, which can beaccessed by chemical synthesis. This facilitates chemical modifications, arequirement for adding function. To achieve our goal, we will test availablepeptide designs and adapt them for our purposes. Currently, we are working withthe well-understood coiled-coil motif and the short WW domain, on which we aimto install unusual binding properties or reactivity. Furthermore, de novo peptidebuilding blocks are used in materials design and functionalization.