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Hyperpolarized water can be a valuable aid in protein NMR, leading to amidegroup 1H polarizations that are orders of magnitude larger than their thermalcounterparts. Suitable procedures can exploit this to deliver 2D 1H-15Ncorrelations with good resolution and enhanced sensitivity. These enhancementsdepend on the exchange rates between the amides and the water, thereby yieldingdiagnostic information about solvent accessibility. This study applied thisHyperW method to four proteins exhibiting a gamut of exchange behaviors: PhoA4,an unfolded 122-residue fragment; barstar, a fully folded ribonucleaseinhibitor; R17, a 13.3 kDa system possessing folded and unfolded forms underslow interconversion; and drkN SH3, a protein domain whose folded and unfoldedforms interchange rapidly and with temperature-dependent population ratios. ForPhoA4 HyperW sensitivity enhancements were larger than 300-fold, as expectedfor an unfolded protein sequence. Though fully folded barstar also exhibitedsubstantial enhancements; these, however, were not uniform, and according toCLEANEX experiments reflected the solvent-exposed residues. R17 showed theexpected superposition of 100-fold enhancements for its unfolded form,coexisting with more modest folded counterparts. Unexpected, however, was thebehavior of drkN SH3, for which HyperW enhanced the unfolded but even morecertain folded protein sites. These preferential enhancements were repeatedlyand reproducibly observed; a number of explanations including three-siteexchange magnetization transfers between water, unfolded and folded states;cross-correlated relaxation processes from hyperpolarized structural waters andlabile sidechain protons; and the possibility that faster solvent exchangerates characterize certain folded sites over their unfolded counterparts areconsidered to account for them.

Assessing site-specific enhancements imparted by hyperpolarized water in folded and unfolded proteins by 2D HMQC NMR