The design of enzyme-like catalysts tests our understanding of sequence-to-structure/function
relationships in proteins. Here we install hydrolytic activity predictably into a completely de …

The design of peptides that assemble in membranes to form functional ion channels is
challenging. Specifically, hydrophobic interactions must be designed between the peptides and at …

Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis,
but identification and analysis of dynamical effects in enzyme-catalyzed reactions have …

Mitophagy, the elimination of mitochondria via the autophagy‐lysosome pathway, is essential
for the maintenance of cellular homeostasis. The best characterised mitophagy pathway is …

Increasingly, it is possible to design peptide and protein assemblies de novo from first
principles or computationally. This approach provides new routes to functional synthetic …

We describe de novo-designed α-helical barrels (αHBs) that bind and discriminate between
lipophilic biologically active molecules. αHBs have five or more α-helices arranged around …

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 …

Our ability to design completely de novo proteins is improving rapidly. This is true of all
three main approaches to de novo protein design, which we define as: minimal, rational and …

An ability to organize and encapsulate multiple active proteins into defined objects and
spaces at the nanoscale has potential applications in biotechnology, nanotechnology, 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-protein …