Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Protein design has come of age, but how will it mature? In the 1980s and the 1990s, the
primary motivation for de novo protein design was to test our understanding of the …

The α-helix is pre-eminent in structural biology and widely exploited in protein folding,
design and engineering. Although other helical peptide conformations do exist near to the α …

The de novo design of proteins that bind highly functionalized small molecules represents a
great challenge. To enable computational design of binders, we developed a unit of protein …

The folding of collagen is a hierarchical process that starts with three peptides associating
into the characteristic triple helical fold. Depending on the specific collagen in question …

As molecular scientists have made progress in their ability to engineer nanoscale molecular
structure, we face new challenges in our ability to engineer molecular dynamics (MD) and …

Differential sensing attempts to mimic the mammalian senses of smell and taste to identify
analytes and complex mixtures. In place of hundreds of complex, membrane-bound G …

The rational design of linear peptides that assemble controllably and predictably in water is
challenging. Short sequences must encode unique target structures and avoid alternative …

Spectrally separated fluorophores allow the observation of multiple targets simultaneously
inside living cells, leading to a deeper understanding of the molecular interplay that …

Proteins are one of the most important and resourceful biomolecules that find applications in
health, industry, medicine, research, and biotechnology. Given its tremendous relevance …