Integrative structural analysis identifies the structural basis and key residues responsible for IDE conformational dynamics that control the unfolding and selective degradation of amyloid peptides.
A range of biophysical techniques is used in combination with computational analysis to understand whether glutamine-binding protein binds its ligand via the induced-fit or conformational selection mechanism.
Empirical substitution matrices from experimental measurements on 31,614 variants accurately predict cellular protein abundance changes using only amino-acid substitution and whether the site is buried or exposed.
Cryo-EM structures unexpectedly show that there are two binding sites for RAB5, with the VPS15 site being the most evolutionarily ancient site, which is essential for endocytic sorting.
