2D NMR spectroscopy of refolding RNase Sa using polarization transfer from hyperpolarized water
 

2D NMR spectroscopy of refolding RNase Sa using polarization transfer from hyperpolarized water

Polarization transfer from hyperpolarized water through proton exchange is used to enhance the NMR signals of amide protons of the Ribonuclease Sa protein. Spectra of the refolding protein are measured within 6 s after dilution of the denaturant urea, at urea-dependent folding rates adjusted in the range of 0.3-0.8 s^(-1). Peak patterns including a mixture of folded and unfolded protein at different ratios are observed. The changes in the observed signals indicate that each spectrum accesses a...

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