Conformational stabilities of the rat alpha- and beta-parvalbumins.

It is widely believed that beta-parvalbumin (PV) isoforms are intrinsically less stable than alpha-parvalbumins, due to greater electrostatic repulsion and an abbreviated C-terminal helix. However, when examined by differential scanning calorimetry, the apo-form of the rat beta-PV (i.e. oncomodulin) actually displays greater thermal stability than the alpha-PV. Whereas the melting temperature of the a isoform is 45.8 degrees C at physiological pH and ionic strength, the Tm for the beta isoform is more than 7 degrees higher (53.6 degrees C). This result suggests that factors besides net charge and C-terminal helix length strongly influence parvalbumin conformational stability. Extension of the F helix in the beta-PV, by insertion of Ser-109, has a modest stabilizing effect, raising the Tm, by 1.1 degrees. Truncation of the alpha-PV F helix, by removal of Glu-108, has a more profound impact, lowering the Tm by 4.0 degrees.