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. 2020 Sep 22;21(18):6949. doi: 10.3390/ijms21186949

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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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pK_a and hydrophobic effects on the observed hyper-reactivity in a reduced lysozyme. (A) Experimental kinetic data for the reaction of rLyz with CDNB and NBD-Cl at pH = 7.4, normalized to those of an unperturbed protein cysteine (enhanced reactivity) [13]. (B) Enhanced reactivity due to the experimental lower pK_a for four cysteines (pK_a = 7.1). (C) Enhanced reactivity due to hydrophobic interaction. (D) The circle diagrams show the percent contribution of the two factors: the hydrophobic effect (blue) and the pK_a effect (red). The 100% represents the sum of the values reported in panels (B,C). The error bars in panels (A–C) are derived from the propagation of uncertainties (see Section 4).