Liquid water is vital to protein structure and stability, yet our understanding of how water shapes proteins is far from comprehensive. Our incomplete knowledge of this fundamental relationship is due in part to the long-standing technological inability to experimentally assess, at high resolution, protein-water interactions and how their absence – i.e., dehydration – impacts protein structure. It is now possible to obtain residue-level information on dehydrated protein structure via Liquid-Observed Vapor Exchange (LOVE) NMR, a solution NMR technique that quantifies the extent of hydrogen-deuterium exchange between the backbone amide protons of a dehydrated protein and D2O vapor. In this talk, I will explain the principles behind LOVE NMR and show how we applied this method to link mutation-induced changes in dehydrated protein structure to changes in solution structure and stability. I will then demonstrate how LOVE NMR was used to probe the mechanism of dehydration protection by disordered proteins derived from anhydrobiotic organisms. I will conclude with a discussion of the future of LOVE NMR and the implications of our findings for the long-term storage of biologic drugs.

LOVE NMR reveals how (de)hydration influences protein structure and stability at the residue level

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