. Author manuscript; available in PMC: 2009 Jun 8.

Published in final edited form as: Biochemistry. 2008 Jan 18;47(9):2968–2977. doi: 10.1021/bi701923h

Table 2.

Parameters of GdnHCl-induced denaturation, KI quenching, and fluorescence anisotropy of apoE single Trp mutants at 25 °C^a

apoE variant	Thermodynamic parameters of denaturation			Quenching by KI^b		Flurorescene anisotropy
apoE variant	ΔG_D°	D_1/2	m	f_a	K_sv	Flurorescene anisotropy
	kcal/mol	M	kcal/mol apoE/mol GdnHCl		M⁻¹
apoE3 W@264	1.4 ± 0.1	0.53 ± 0.02	2.7 ± 0.3	0.52 ± 0.03	13.6 ± 1.3	0.084 ± 0.005
apoE4 W@264	1.3 ± 0.1	0.52 ± 0.02	2.5 ± 0.2	0.59 ± 0.02	14.9 ± 0.7	0.078 ± 0.004
apoE3 (1–272) W@264	0.6 ± 0.1	0.38 ± 0.03	1.6 ± 0.3	0.62 ± 0.02	7.8 ± 0.4	0.058 ± 0.003
apoE4 (1–272) W@264	0.6 ± 0.1	0.31 ± 0.04	1.8 ± 0.4	0.58 ± 0.05	13.1 ± 1.6	0.064 ± 0.004

Values are drived from duplicate or triplicate measurements from at least two independent preparations of proteins.

Parameters of Trp fluorescence quenching: f_a, fraction of Trp residue accessible to I⁻; K_sv, Stern-Volmer constant.