In most cases, protein aggregation stems from the establishment of non-native
intermolecular contacts. The formation of insoluble protein aggregates is associated with …

Protein aggregation is a topic of immense interest to the scientific community due to its role
in several neurodegenerative diseases/disorders and industrial importance. Several in silico …

The amyloid conformation can be adopted by a variety of sequences, but the precise
boundaries of amyloid sequence space are still unclear. The currently charted amyloid …

Spider silk—an environmentally friendly protein‐based material—is widely recognized for its
extraordinary mechanical properties. Biomimetic spider silk‐like fibers made from …

Amyloid fibrils—nanoscale fibrillar aggregates with high levels of order—are pathogenic in
some today incurable human diseases; however, there are also many physiologically …

Stress granules are ribonucleoprotein assemblies that form in response to cellular stress.
Many of the RNA-binding proteins found in stress granule proteomes contain prion-like …

Amyloids are unbranched protein fibrils with a characteristic spatial structure. Although the
amyloids were first described as protein deposits that are associated with the diseases …

In classical amyloidoses, amyloid fibres form through the nucleation and accretion of protein
monomers, with protofibrils and fibrils exhibiting a cross-β motif of parallel or antiparallel β …

Several computational methods have been developed to predict amyloid propensity of a
protein or peptide. These bioinformatics tools are time-and cost-saving alternatives to …

Protein and peptide aggregation has recently become one of the most studied biomedical
problems due to its central role in several neurodegenerative disorders and of …