TABLE 2.

Percent α-helical, β-sheet, and random conformations of different mutants of NSP4 from Hg18 and SA11 strains^a

Mutant	Content (%)			Tm (°C)
	α-Helix	β-Sheet	Random coil
Hg18ΔN72	62	6	31	>81
Hg18ΔN85	47	22	31	43
Hg18ΔN94	45	23	31	44
Hgm1	45	23	31	55
Hgm3	44	23	31	∼68
Hgm6	45	23	31	∼66
Hgm15	47	20	32	∼66
SA11ΔN72	61	7	32	>80
SA11ΔN85	47	21	32	44
SA11dirm1	59	8	33	∼70
SA11dirm2	46	23	31	∼71
SA11dirm3	45	23	32	∼72
SA11dirm4	53	14	33	∼77

^aNote that both N- and C-terminal mutants of ΔN72 exhibit properties, except for T_m values, similar to those of ΔN85 which lacks AAH_73-85. The G140A mutant dirm1 exhibits similar α-helical and β-sheet conformation contents but a different T_m value compared to ΔN72. Among all the mutants, ΔN72 from both strains exhibits the highest α-helical and least β-sheet contents. The T_m values of the ΔN72, Hgm3, Hgm6, Hgm15, and DIR mutants represent approximate values since the proteins exhibit incomplete thermal unfolding profiles that are distinct from each other.