. 2017 Sep 6;2(9):5504–5517. doi: 10.1021/acsomega.7b00703

Table 1. Fluorescence Quenching Data and Binding Parameters of nfx^± (at pH 7.2) or nfx^– (at pH 9.2) with Lysozyme at 298 K.

system	K_SV (L mol^–1)	k_q (L mol^–1 s^–1)	K (mol L^–1)	n	ΔG° (kJ mol^–1 K^–1)
nfx^±–lyz	(3.5 ± 0.03) × 10⁴	(4.08 ± 0.03) × 10¹³	(1.73 ± 0.1) × 10⁴	(0.94 ± 0.02)	–24.18
nfx^––lyz	(1.4 ± 0.07) × 10⁴	(1.91 ± 0.07) × 10¹³	(2.40 ± 0.3) × 10³	(0.86 ± 0.02)	–19.28

Table 1. Fluorescence Quenching Data and Binding Parameters of nfx± (at pH 7.2) or nfx– (at pH 9.2) with Lysozyme at 298 K.