Table 1. Stability of the α-SH3 with amyloidogenic insertions as estimated by thermal denaturation monitored by CD.

Protein*	Tm,† K	ΔGu,† Kcal/mol	Denatured protein,† %	Folded protein,† %
WT	321.5 ± 0.3	1.39 ± 0.05	8.7 ± 0.7	91.3 ± 0.7
1-SH	319.0 ± 0.3	1.46 ± 0.07	7.9 ± 0.8	92.1 ± 0.8
2-SH	—‡	—‡	—‡	—‡
3-SH	316.9 ± 0.2	1.32 ± 0.05	9.7 ± 0.7	90.2 ± 0.7
Aβ-SH	319.7 ± 0.2	1.61 ± 0.05	7.0 ± 0.6	93.0 ± 0.6
SH-1	313.0 ± 0.6	0.77 ± 0.04	21.7 ± 1.2	78.3 ± 1.2
SH-2	313.4 ± 0.4	0.96 ± 0.05	16.7 ± 1.2	83.3 ± 1.2
SH-3	321.5 ± 0.3	0.94 ± 0.04	17.4 ± 0.9	82.6 ± 0.9
SH-Aβ	322.2 ± 0.2	1.54 ± 0.05	6.1 ± 0.5	93.9 ± 0.5
AmyBergerac	—‡	—‡	—‡	—‡

Protein variants that form amyloid fibrils are in italics.

^*Thermal denaturation has been performed on freshly prepared protein solutions (pH 2.6, c = 50 μM).

^†Stability parameters and errors have been calculated as explained in Materials and Methods.

^‡Nonreversible transition.