The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

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 …

Natural metalloproteins perform many functions—ranging from sensing to electron transfer
and catalysis—in which the position and property of each ligand and metal are dictated by …

Proteins are molecular machines whose function depends on their ability to achieve
complex folds with precisely defined structural and dynamic properties. The rational design …

Histidine, a versatile proteinogenic amino acid, plays a broad range of roles in all living
organisms and behaves as a key mediator of the interactions of biomolecules with inorganic …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Self-assembly of molecules often results in new emerging properties. Even very short
peptides can self-assemble into structures with a variety of physical and structural …

Inflammatory responses, manifested in excessive oxidative stress and microglia
overactivation, together with metal ion-triggered amyloid-beta (Aβ) deposition, are critical …

Enzymatic activity is crucial for various technological applications, yet the complex structures
and limited stability of enzymes often hinder their use. Hence, de novo design of robust …