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. 2020 Nov 3;10(4):207. doi: 10.3390/jpm10040207

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Local stability of the N-terminal domain (NTD) probed by proteolysis with thermolysin. (A) Location of mutated residues regarding the thermolysin cleavage site (TCS). The minimal distance between the mutated residue and the TCS backbone (Ser72-Val73) is also indicated (using the structure with PDB code 2F1O). (B) Linear dependence of apparent rate constants (k_obs) on protease concentration. The slopes provide the values of the second-order rate constants k_prot. (C,D) Values of k_prot for the NQO1 variants (C) and the effect of mutations on the local stability (D) as ΔΔG_prot. Note that a positive value of ΔΔG_prot indicates a destabilizing effect.