Finding the wet spots

摘要

Proteins in cells are responsible for the vast majority of biological functions. Because life evolved in water, protein molecules are uniquely adapted to use their aqueous environments to facilitate their func-tions. Yet remarkably little is known about the interactions between solvent water and protein molecules, or how those interactions affect (or are affected by) the conformational changes at the heart of protein function. In Nature Structural and Molecular Biology, Nucci et al. now report that nuclear magnetic resonance (NMR) spectroscopy of proteins encapsulated in reverse micelles - cell-like compartments in which nanometre-scale pools of water are surrounded by a membrane - can provide a comprehensive picture of how water molecules bind to proteins. This picture not only chal-lenges current dogma about protein hydration, but also promises to illuminate key aspects of the relationship between protein and water dynamics, and of how proteins use water to perform their functions.