Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Protein-protein interactions (PPIs) mediate a variety of cellular processes and form complex
networks, where connectivity is achieved owing to the “hub” proteins whose interaction with …

A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …

DNA trinucleotide repeats (TRs) can exhibit dynamic expansions by integer numbers of
trinucleotides that lead to neurodegenerative disorders. Strand slipped hairpins during DNA …

Amino acids have emerged as promising molecular frameworks for the generation of
functional materials owing to the bio-compatibility and thermodynamic stability of their self …

Curli are amyloid fibrils that grow from many enteric bacteria and play a structural role in the
biofilm extracellular matrix (ECM). Although curli biogenesis is one of the best understood …

Amyloid aggregation and human disease are inextricably linked. Examples include
Alzheimer disease, Parkinson disease, and type II diabetes. While seminal advances on the …

AD is a progressive and irreversible neurodegenerative disease and the most common
cause of dementia in the elderly population. eta-amyloid cascade formation along with …

Amyloids are supramolecular assemblies composed of polypeptides stabilized by an
intermolecular beta-sheet core. These misfolded conformations have been traditionally …

Proteins and peptide fragments are highly relevant building blocks in self-assembly for
nanostructures with plenty of applications. Intrinsically disordered proteins (IDPs) and …