“…This means that hydrophobic interactions between the α-helices of lipid free apoA-I might not contribute substantially to the thermodynamic stability of the monomeric state. In conclusion, the thermodynamic properties of lipid free apoA-I at plasma concentrations should be typical for a molten globular state, i.e., the protein has a compact folding, with a core of α-helices bundled via hydrophobic contacts (Barbeau et al, 1979 ; Atkinson and Small, 1986 ; Nolte and Atkinson, 1992 ; Gursky and Atkinson, 1996 ), a reduced cooperative unfolding (Reynolds, 1976 ; Gursky and Atkinson, 1996 ), lacks a defined tertiary structure, has increased solvent access to its hydrophobic surfaces (Reynolds, 1976 ; Rosseneu et al, 1977 ; Gursky and Atkinson, 1996 ), is easily denatured, has high affinity for hydrophobic ligands, and a predisposition to form aggregates (Reynolds, 1976 ; Tall et al, 1976 ).…”