Table 1.

α-helix content and thermal denaturation parameters of apoE3 C-terminal truncated mutants

apoE3 variant	α-helixa	number of residues in α-helix	Tmb	Cooperativity index	ΔHvc
	%	amino acids	°C		kcal/mol
apoE3	45 ± 3	131	47	2.6	22
apoE3 (1–272)	40 ± 2	109	58	N.D.d	N.D.d
apoE3 (1–260)	38 ± 2	101	57	7.5	33
apoE3 (1–250)	40 ± 3	101	60	13	49
apoE3 22-kDa	47 ± 4	91	51	3.6	24

^aMean ± S.D. from at least three measurements.

^bThe reproducibility in T_m is ± 1.5 °C.

^cEstimated error is ± 2 kcal/mol.

^dThermal denaturation was not cooperative.