In water, simulations indicate that DyHes are largest around 220K. This temperature however depends on the model used and it has been difficult to measure experimentally pure liquid water dynamics in this temperature due to freezing. Interestingly, at the same temperature occurs the so-called protein ‘glass’ transition. Around this temperature many proteins lose their conformational flexibility and biological function. Is this transition due to the intrinsic temperature dependence of the protein motion or is it dictated by DyHes in the surrounding water molecules?
This project aims to unveil experimentally DyHes in prototype glass-formers, aqueous solutions and hydrated protein dynamics. The purpose is to resolve the long-lasting question related to the origin of the protein ‘glass’ transition, which will have major implications in understanding enzymatic activity and protein folding. The experiments utilize novel coherent x-ray diffraction techniques in new x-ray sources, such as the Swedish synchrotron MAX IV and the European X-ray Free-Electron Laser which are only recently available. As such, the long-term impact of the proposed investigations is to train scientists to use these new technologies.