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 aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

The formation of amyloid aggregates upon protein misfolding is related to several
devastating degenerative diseases. The propensities of different protein sequences to …

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

The evolution of antibiotic-resistant bacteria is an ongoing and troubling development that
has increased the number of diseases and infections that risk going untreated. There is an …

The purpose of this work was to construct a consensus prediction algorithm of 'aggregation-
prone'peptides in globular proteins, combining existing tools. This allows comparison of the …

Polymorphism is a key feature of amyloid fibril structures but it remains challenging to
explain these variations for a particular sample. Here, we report electron cryomicroscopy …

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 …

Amyloids are protein aggregates with a highly ordered spatial structure giving them unique
physicochemical properties. Different amyloids not only participate in the development of …

The aggregation of proteins or peptides in amyloid fibrils is associated with a number of
clinical disorders, including Alzheimer's, Huntington's and prion diseases, medullary thyroid …