The interactions of proteins with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been difficult. Confinement within the nanoscale interior of a reverse micelle allows detection of protein-water interactions using solution NMR techniques. Complications that normally arise from short residence times, hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle sample. Characterization of ubiquitin  demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of NOE and ROE intensities indicate a considerable range of hydration water dynamics on the protein surface. A clustering of different hydration dynamics is evident. These clusters also correlate with the surface that is involved in protein-protein interactions suggesting that evolution has maximized the hydrophobic effect (i.e. entropy gain of water). Studies of other proteins will also be presented.

Site-resolved measurement of water-protein interactions by solution NMR

243rd National Meeting (2012)

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