NMR study of the unfolding of ribonuclease A, and dynamical studies of liquids in confined geometries
The cold, heat, and pressure unfolding of RNase A has been studied by 1D and 2D $\sp1$H NMR spectroscopy, spin-lattice relaxation time measurements, and the pressure-jump hydrogen-exchange method. It was found that the pressure denatured states of RNase A display some characteristics of a molten globule, and all three $\alpha$-helices and the $\beta$-sheet of the native protein remain partially folded structures in the pressure denatured state. $\sp1$H spectra of the denatured RNase A suggest that the cold and pressure denatured states are more structured than the heat denatured state, while the cold denatured state is more structured than the pressure denatured state.
University of Illinois - Urbana-Champaign
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University of Illinois at Urbana-Champaign