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. Author manuscript; available in PMC: 2013 Nov 6.
Published in final edited form as: Biochemistry. 2012 Oct 24;51(44):8993–9001. doi: 10.1021/bi300926j

TABLE 1.

Influence of Iowa and Milano mutations on apoA-I physical properties

Parameter Wild-type Iowa Milanoa
Change in α-helix content (%)b - −12 −2
Relative ANS binding 1.0 1.5 1.6
Free energy of denaturation (kcal/mol)c 3.5 ± 0.1 2.4 ± 0.1 2.4 ± 0.2
a

The data for the monomer (reduced) form are from ref. (14).

b

The α-helix content of wild-type apoA-I was 49 ± 5% and varied somewhat with sample history.

c

CD was employed to monitor the loss of α-helix content when apoA-I was exposed to increasing concentrations of GdmCl.