Frederic Rousseau

TL;DR: The core functionality of FoldX, namely the calculation of the free energy of a macromolecule based on its high-resolution 3D structure, is now publicly available through a web server at FoldX.

TL;DR: Waltz as mentioned in this paper is a web-based tool that uses a position-specific scoring matrix to determine amyloid-forming sequences, which allows users to identify and better distinguish between Amyloid sequences and amorphous beta-sheet aggregates.

TL;DR: It is shown that small alterations in the Aβ42:Aβ40 ratio dramatically affect the biophysical and biological properties of the A β mixtures reflected in their aggregation kinetics, the morphology of the resulting amyloid fibrils and synaptic function tested in vitro and in vivo.

TL;DR: The analysis of the beta aggregation propensity of all-alpha, all-beta and mixed alpha/beta globular proteins as well as membrane-associated proteins is fairly similar, illustrating firstly that globular structures possess an appreciable amount of structural frustration and secondly that beta-aggregation is not determined by hydrophobicity and beta-sheet propensity alone.

TL;DR: Computational and experimental work shows that preventing aggregation does not necessarily mean that amyloid formation is prevented and vice versa, and it seems that gatekeeper residues are also important in determining chaperone selectivity for strongly aggregating regions.