. 2018 Jun 27;74(Pt 7):681–689. doi: 10.1107/S2059798318007878

Table 3. Thermodynamic parameters of interaction between EBOV NP^Ct mutants and MJ20 with the corresponding melting temperatures (T _m) of each mutant.

Thermodynamics were evaluated using isothermal titration calorimetry, while scanning fluorescence was used to determine the melting temperatures (T _m). Alanine substitution has little effect on the affinity for MJ20; however, the loss of the side chain influenced the stability of the antigen.

sFab MJ20–EBOV NP^Ct complex	K _d (nM)	ΔH (kcal mol⁻¹)	−TΔS (kcal mol⁻¹)	ΔG (kcal mol⁻¹)	T _m (°C)
Wild type	3.66	−31.15	19.65	−11.50	56.9
Y652A	18.0	−30.49	19.95	−10.54	50.9
L656A	10.0	−29.72	18.81	−10.91	52.7
S679A	7.41	−30.36	19.26	−11.10	56.0
S681A	12.0	−28.28	17.47	−10.81	57.3
M732A	32.0	−29.90	16.70	−10.20	54.0
L735A	103.5	−28.10	18.57	−9.52	47.8

Table 3. Thermodynamic parameters of interaction between EBOV NPCt mutants and MJ20 with the corresponding melting temperatures (T m) of each mutant.

Table 3. Thermodynamic parameters of interaction between EBOV NP^Ct mutants and MJ20 with the corresponding melting temperatures (T _m) of each mutant.