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In PNAS, Nucci et al. (1) present an NMR study suggesting the pressure-induced denaturation of individual domains of the T4 lysozyme mutant Leu99Ala (T4L L99A). The denaturation equilibrium was considered to be responsible for the pressure-induced loss of 15N-1H heteronuclear single quantum coherence (HSQC) cross-peaks, which were preferentially observed for residues in the C-terminal domain. Independently, our laboratories have studied the L99A mutant by high-pressure NMR spectroscopy (2). In the study of Nucci et al., the signal intensity was taken to be proportional to the population of the folded state and used to derive the equilibrium for unfolding at …

Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T 4 lysozyme due to unfolding?

Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T ₄ lysozyme due to unfolding?