Figure 2
From: A human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding
The L253P ABD has intact secondary structures but decreased thermal stability.
(A) A Coomassie blue stained gel containing 2 μg of purified wild-type (WT) or L253P ABD protein resolved by SDS-PAGE. The β-III-spectrin ABD (amino acids 1–284) has a predicted molecular weight of 32.8 kDa and runs between the 28 and 41 kDa protein standards. A minor protein contaminant runs below the 28 kDa protein standard. (B) Circular dichroism spectra between 200 and 260 nm for the wild-type and L253P ABD proteins show pronounced alpha-helical profiles. (C) Circular dichroism melting curve analyses at 222 nm for wild-type and L253P ABD proteins show sharp, cooperative unfolding transitions. The L253P ABD has a melting temperature (Tm) that is 15 °C lower than wild-type.
