Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for
their robust material properties and inherent biological compatibility as well as their putative …

Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety
of different proteins. These assemblies have received much interest in recent decades, due …

Solubility is a key requirement for the functioning of a protein within the complex network of
cellular components.[1–4] A class of highly debilitating disorders, including Alzheimer s and …

Lysozyme is associated with hereditary systemic amyloidosis in humans. Hen egg white
lysozyme (HEWL) has been extensively studied as an amyloid forming protein. In this study …

Conformational diseases constitute a group of heterologous disorders in which a constituent
host protein undergoes changes in conformation, leading to aggregation and deposition. To …

To contribute to the question of the putative role of cystatins in Alzheimer disease and in
neuroprotection in general, we studied the interaction between human stefin B (cystatin B) …

Here we discuss studies of the structure, folding, oligomerization and amyloid fibril formation
of several proline mutants of human stefin B, which is a protein inhibitor of lysosomal …

Similar to other polypeptides and electrolytes, proteins undergo phase transitions, obeying
physicochemical laws. They can undergo liquid-to-gel and liquid-to-liquid phase transitions …

Mutations in the gene for human stefin B (cystatin B) cause progressive myoclonic epilepsy
type 1 (EPM1), a neurodegenerative disorder. The most common change is dodecamer …

Human cystatin C (hCC) is a small but very intriguing protein. Produced by all nucleated
cells is found in almost all tissues and body fluids where, at physiological conditions, plays a …