Protein and hydration-water dynamics are decoupled: A new model connecting dynamics and biochemical function is required

Abstract

Water plays a major role in bio-systems, greatly contributing to determine their structure, stability and even function. It is well know, for instance, that proteins require a minimum amount of water to be functionally active. Since the biological functions of proteins involve changes of conformation, and sometimes chemical reactions, it is natural to expect a connection of these functions with dynamical properties of the coupled system of proteins and their hydration water. However, despite many years of intensive research, the detailed nature of protein - hydration water interactions, and their effect on the biochemical activity of proteins through peculiar dynamical effects, is still partly unknown. In particular, models proposed so far, fail to explain the full set of experimental data. The well-accepted 'protein dynamical transition' scenario is based on perfect coupling between the dynamics of proteins and of their hydration water, which has never been confuted experimentally. We present high-energy resolution elastic neutron scattering measurements of the atomistic dynamics of the model protein, lysozyme, in water that were carried out on the IN16B spectrometer at the Institut Laue-Langevin in Grenoble, France. These show for the first time that the dynamics of proteins and of their hydration water are actually de-coupled. This important result militates against the well-accepted scenario, and requires a new model to link protein dynamics to the dynamics of its hydration water, and, in turn, to biochemical function.