Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

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 …

The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …

Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

Intermediate species in the assembly of amyloid filaments are believed to play a central role
in neurodegenerative diseases and may constitute important targets for therapeutic …

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 …

A wide range of proteins have been reported to condensate into a dense liquid phase,
forming a reversible droplet state. Failure in the control of the droplet state can lead to the …

Alzheimer's disease is the most common neurodegenerative disease, and there are no
mechanism-based therapies. The disease is defined by the presence of abundant …

Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …