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Solution Structure of a Repeated Unit of the ABA-1 Nematode Polyprotein Allergen of Ascaris Reveals a Novel Fold and Two Discrete Lipid-Binding Sites

Figure 2

Reduced thermal stability of recombinant ABA-1A upon removal of resident ligand(s).

Differential scanning calorimetry (DSC) data showing the higher thermal stability of rABA-1A compared to the same protein (RP-ABA-1A) after treatment to remove endogenous ligands. This is consistent with the presence of bound endogenous ligands stabilizing the native conformation of the recombinant protein.

Figure 2

doi: https://doi.org/10.1371/journal.pntd.0001040.g002