. Author manuscript; available in PMC: 2013 Mar 1.

Published in final edited form as: Biochim Biophys Acta. 2011 Aug 5;1821(3):456–463. doi: 10.1016/j.bbalip.2011.07.020

Table 2.

α-Helix content and parameters of thermal denaturation and ANS binding of human apoA-I C-terminal variants

apoA-I variant	α-Helix^a (%)	T_m^b (°C)	ΔH_v^c (kcal/mol)	ANS fluorescence^d
WT	52 ± 1	59	33	1.0
F225L/F229A/Y236A	52 ± 2	57	44	0.5
F225L/F229L/A232L/Y236L	55 ± 4	56	23	1.1

Mean ± SD from at least three experiments.

The reproducibility in midpoint temperature T_m is ± 1.5°C.

Van’t Hoff enthalpy. Estimated error is ± 0.5kcal/mol.

Values are relative to WT. Estimated error is within ± 0.1.