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 …

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 …

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

Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …

The use of transgenic mice displaying amyloid-β (Aβ) brain pathology has been essential for
the preclinical assessment of new treatment strategies for Alzheimer's disease. However, the …

The prediction of highly ordered three-dimensional structures of amyloid protein fibrils from
the amino acid sequences of their monomeric self-assembly precursors constitutes a …

The assembly of proteins into fibrillar amyloid structures was once considered to be
pathologic and essentially irreversible. Recent studies reveal amyloid-like structures that …

Amyloid fibrils are supramolecular systems showing distinct chirality at different levels of
their complex multilayered architectures. Due to the regular long‐range chiral organization …

The CABS model can be applied to a wide range of protein-protein and protein-peptide
molecular modeling tasks, such as simulating folding pathways, predicting structures …

The aggregation of amyloid-β protein (Aβ) into oligomers and amyloid fibrils is closely
related to Alzheimer's disease (AD). Aβ40 and Aβ42, as two most prominent isoforms of Aβ …