Understanding the atomistic resolution changes during the self-assembly of amyloid
peptides or proteins is important to develop compounds or conditions to alter the …

The accumulation of pathogenic protein oligomers and aggregates is associated with
several devastating amyloid diseases. As protein aggregation is a multi-step nucleation …

Protein aggregation can produce a wide range of states, ranging from fibrillar structures and
oligomers to unstructured and semistructured gel phases. Recent work has shown that many …

Atomic characterization of large nonfibrillar aggregates of amyloid polypeptides cannot be
determined by experimental means. Starting from β‐rich aggregates of Y and elongated …

Many biological functions are mediated by large complexes formed by multiple proteins and
other cellular macromolecules. Recent progress in experimental structure determination, as …

Structure-based models have been instrumental in simulating protein folding and
suggesting hypotheses about the mechanisms involved. Nowadays, at least for fast-folding …

Pathological aggregation of essentially dissociative Transthyretin (TTR) monomers protein,
driven by misfolded and self-interaction, is connected with Amyloid Transthyretin …

Proteins are complex biopolymers responsible for key functions in plant, microbial, fungal,
and animal organisms. Due to the variability induced by the chemical composition of the 20 …

Amyloidosis is a systemic disease, leading to the disfunction of many organs. There are
several clinical and morphological forms of amyloidosis based on the organ-specific nature …

The computational study of the binding of a ligand to a target protein provides mechanistic
insight into the molecular determinants of this process and can improve the success rate of …