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February 2019:
Congratulations to Jihyun Kim for winning Best Poster Award at the Minerva-Gentner Symposium on MR Spectroscopy & Molecular Imaging

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Protein Hydration

Scheme of protein structure with interacting water moleculeProtein–solvent interactions are recognized as important factors in protein structure, dynamics, and function. NMR as a method for structural biology has the ability to study proteins in an aqueous environment. Here, we utilize hyperpolarized water to facilitate the measurement of polarization transfer from water to protein. Because polarization transfer efficiency is governed by the molecular structure and dynamics, its measurement can give insight into these fundamental molecular properties.Scheme of protein structure with interacting water molecule Hyperpolarization enhances the changes of the protein NMR signal observed due to exchange of labile protons, and due to cross-relaxation. The signal buildup and decay curves shown in the figure represent the typical time dependence observed as a result of these processes. In this case, fitting with a three-site model involving signal intensities of water, amide, and aliphatic protons enables to determine the overall water-amide proton exchange rate (kex), as well as overall intramolecular cross-relaxation rate (σ).