Water is largely considered to be indispensable to life. But a molecular understanding of the role played by water in the biochemical function of proteins and DNA has long remained elusive. Recent experimental and theoretical works have lead to a detailed description of the water hydrogen-bond network dynamics and of its changes in the presence of simple solutes. These new results now open the way to the challenging study of the water behavior in complex biochemical environments. We will show that numerical simulations and theoretical modeling established in prior studies of smaller solutes provide a molecular description of protein and DNA hydration dynamics. In agreement with experimental observations, the hydration shell is found to be slower than bulk water, and the molecular origin of this slowdown can be now precisely identified. Whether this slowdown is rather due to the shape of the biomolecule or to its chemical exposed groups is determined unambiguously.<br/>In a complementary study, we will focus on the influence of water on the function of proteins, to understand why the presence of water enhances the catalytic activity of enzymes. Water is usually depicted as a lubricant which facilitates the conformational transitions occurring during enzyme catalysis. Through the study of a paradigm enzyme in a non-aqueous solvent, we will assess the molecular validity of this description and suggest new routes to optimize the enzymatic catalytic activity in non-aqueous solvents.

Biomolecular hydration shells: Dynamics and effect on biochemical function

253rd National Meeting (2017)

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