The artificial intelligence program AlphaFold 2 is revolutionizing the field of protein structure
determination as it accurately predicts the 3D structure of two thirds of the human proteome …

Homorepeats (or polyX), protein segments containing repetitions of the same amino acid,
are abundant in proteomes from all kingdoms of life and are involved in crucial biological …

The self-assembly of metal-organic cages enables the rapid creation of atomically defined,
three-dimensional, nanoscale architectures reminiscent of proteins. However, existing metal …

Glycine-rich regions feature prominently in intrinsically disordered regions (IDRs) of proteins
that drive phase separation and the regulated formation of membraneless biomolecular …

Hydrogen bond cooperativity (HBC) plays an important role in stabilizing protein assemblies
built by α-helices and β-sheets, the most common secondary structures. However, whether …

Proline is a unique amino acid in that its side-chain is cyclised to the backbone, thus giving
proline an exceptional rigidity and a considerably restricted conformational space …

Glycine rich polyproline II helix assemblies are an emerging class of natural domains found
in several proteins with different functions and diverse origins. The distinct properties of …

The use of polyproline II (PPII) helices in protein design is currently hindered by limitations in
our understanding of their conformational stability and folding. Recent studies of the snow …

The incorporation of fluorinated amino acids into proteins provides new opportunities to
study biomolecular structure‐function relationships in an elegant manner. The available …

Intrinsically disordered proteins are a class of proteins that lack stable folded conformations
and instead adopt a range of conformations that determine their biochemical functions. The …