Table 1.

α-Helix content and Gdn·HCL denaturation of human plasma apoAI and recombinant deletion mutants in the lipid-free state and in discoidal rHDL

Apolipoprotein*	α-helix content,† %		No. of amino acids in α-helices‡		D1/2,§ M Gdn·HCl		ΔGD°, ¶ kcal/mol apoAI
	Lipid-free	rHDL	Lipid-free	rHDL	Lipid-free	rHDL	Lipid-free	rHDL
Plasma apoAI	57 ± 3	80 ± 6	139	194	1.2 ± 0.2	3.1 ± 0.5	2.5 ± 0.9	2.4 ± 0.5
apoAI Δ44-126	27 ± 2	59 ± 19	43	96	0.8 ± 0.4	2.5 ± 0.2	1.0 ± 0.1	1.7 ± 0.1
apoAI Δ139-170	54 ± 9	68 ± 0	114	143	0.9 ± 0.2	2.8 ± 0.2	1.4 ± 0.2	1.8 ± 0.2
apoAI Δ190-243	56 ± 7	63 ± 3	106	120	1.8	1.7	2.4	1.2

^*Values in this table are derived from triplicate measurements from two independent reconstitution experiments except for the apoAI Δ190-243 (n = 1). 

^†Determined from molar ellipticities at 222 nm (±1 SD). 

^‡Calculated by multiplying the number of amino acids in the protein by the α-helix content. 

^§Gdn·HCl concentration for the protein to become 50% denatured (±1 SD). 

^¶Standard change in free energy of denaturation (±1 SD).