The amylome is the universe of proteins that are capable of forming amyloid-like fibrils. Here
we investigate the factors that enable a protein to belong to the amylome. A major factor is …

The Rosetta software for macromolecular modeling, docking and design is extensively used
in laboratories worldwide. During two decades of development by a community of …

Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological
hallmark of Alzheimer’s disease. Aβ molecules form β-sheet containing structures that …

Subcellular membraneless assemblies are a reinvigorated area of study in biology, with
spirited scientific discussions on the forces between the low-complexity protein domains within …

Growing well‐diffracting crystals constitutes a serious bottleneck in structural biology. A
recently proposed crystallization methodology for “stubborn crystallizers” is to engineer surface …

In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'.
However, it is unclear how a protein conformation can be stable enough to …

β-Cell dysfunction is an important factor in the development of hyperglycemia of type-2 diabetes
mellitus, and pancreatic islet amyloidosis (IA) has been postulated to be one of the main …

Amyloid diseases, including Alzheimer's and prion diseases, are each associated with
unbranched protein fibrils. Each fibril is made of a particular protein, yet they share common …

A very small number of natural proteins have folded configurations in which the polypeptide
backbone is knotted. Relatively little is known about the folding energy landscapes of such …

It has long been known that toxins produced by Bacillus thuringiensis (Bt) are stored in the
bacterial cells in crystalline form. Here we describe the structure determination of the Cry3A …