Abstract

Amyloid oligomers, small aggregates of misfolded proteins, are important in many human diseases, such as type II diabetes. Despite their importance in disease, amyloid oligomers are poorly understood, due to both transient and polymorphic behaviour making experimental characterisation challenging. Therefore, computational studies of amyloid oligomers have become valuable tools with which to extract structural, thermodynamic and kinetic properties. In this talk I will explain an improved step-taking scheme in global optimisation of proteins, and the application of this scheme to locate low-energy conformations of amyloid oligomers. These low-energy conformations can provide starting points for calculating potential energy landscapes, examples of which will be shown for two sets of amyloid oligomers.