Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Recent evidence indicates that diverse neurodegenerative diseases might have a common
cause and pathological mechanism—the misfolding, aggregation and accumulation of …

The ability of proteins to fold to their functional states following synthesis in the intracellular
environment is one of the most remarkable features of biology. Substantial progress has …

The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not
β‐sheet‐containing proteins, such as transthyretin, are predisposed to form such fibrils …

Increasing evidence indicates that many peptides and proteins can be converted in vitro into
highly organised amyloid structures, provided that the appropriate experimental conditions …

Amyloid fibrils and prions are proteinaceous aggregates that are based on a unique form of
polypeptide configuration, termed cross-β structure. Using a group of chemically distinct …

Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD), and electron
microscopy (EM) have been used simultaneously to follow the temperature-induced …

Methods predicting protein secondary structure improved substantially in the 1990s through
the use of evolutionary information taken from the divergence of proteins in the same …

Elastin provides extensible tissues, including arteries and skin, with the propensity for elastic
recoil, whereas amyloid fibrils are associated with tissue-degenerative diseases, such as …

We have systematically studied the effects of 40 single point mutations on the conversion of
the denatured form of the α/β protein acylphosphatase (AcP) into insoluble aggregates. All …