. 2021 May 27;297(1):100836. doi: 10.1016/j.jbc.2021.100836

Table 6.

Ellipticity (mdeg.cm².dmol⁻¹) values observed for hS2 proteins in low-salt buffer and 2 M urea buffer at 208 and 222 nm by CD spectra

hS2 Proteins	n	0 M urea			2 M urea
hS2 Proteins	n	208 nm	222 nm	222/208	208 nm	222 nm	222/208
hS2^Wt	3	−16.95 ± 0.27	−17.63 ± 0.14	1.04 ± 0.01	−16.95 ± 0.19	−16.43 ± 0.13	0.97 ± 0.01^¶¶¶
hS2^R870H	3	−17.52 ± 0.06	−18.18 ± 0.11	1.04 ± 0.002^§§§	−20.06 ± 0.04	−17.37 ± 0.13	0.86 ± 0.01^{§§§,¶¶¶}
hS2^E924K	3	−16.87 ± 0.60	−17.20 ± 0.48	1.02 ± 0.01^§§§	−19.56 ± 0.21	−17.06 ± 0.16	0.87 ± 0.001^{§§§,¶¶¶}
hS2^E930Δ	3	−16.83 ± 0.32	−17.26 ± 0.26	1.03 ± 0.004^§§§	−20.46 ± 0.03	−15.03 ± 0.12	0.74 ± 0.005^{§§§,¶¶¶}

Statistically significant values were calculated by one-way ANOVA calculated with Tukey’s multiple comparison test with single pooled variance. ‘n’ is equal to the number of independent experiments performed for each CD measurement. ± values are for the SEM for reported values. See Table 7 for analysis of main factors and interactions.

^§p < 0.05, ^§§p < 0.01, ^§§§p < 0.001versus hS2^Wt + 2M Urea.

^¶p < 0.05, ^¶¶p < 0.01, ^¶¶¶p < 0.001 versus respective 0M Urea.