Figure 3 | Scientific Reports

Figure 3

From: Different electrostatic forces drive the binding kinetics of SARS-CoV, SARS-CoV-2 and MERS-CoV Envelope proteins with the PDZ2 domain of ZO1

Figure 3

Left panel—dependence of equilibrium dissociation rate constant (KD) as function of NaCl concentration added to the experimental buffer. Data show that the stability of the complex formed by SARS-CoV-2 E peptide appears to be mostly insensitive to increasing ionic strengths, while an increasing KD is appreciable for SARS-CoV and MERS-CoV peptides at increasing [NaCl]. Center and right panel—dependence of microscopic association (kon) and dissociation (koff) rate constants as function of KD. Lines represent the best fit to a linear equation. R2 values are reported. For both SARS-CoV and SARS-CoV-2 E peptides koff dependences are well described by a linear regression. On the other hand, only the kon dependence of SARS-CoV peptide is well fitted by a linear equation.

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