Figure 2.

Thermodynamic and kinetic stability do not correlate with amyloid propensity. (A) Equilibrium denaturation curves for mβ₂m, hβ₂m, and ΔN6 monitored using tryptophan fluorescence (75 mM sodium phosphate buffer pH 6.2, 25 °C). (B) Unfolding free energies obtained by fitting data in (A) to a two state model (see Table S1). (C) Representative hydrogen exchange profiles for the amide hydrogen of residue 83 in hβ₂m, mβ₂m, and ΔN6 at 25 °C and pH 6.2 (see Figure S2).