Type 2B mutations destabilize purified AIM-A1. Locations of represented type 2B mutations on the 3-dimensional crystal structure (PDB:7A6O aligned with PDB:1SQ0 GPIb chain) (A) and linearized schematic on AIM-A1 (B). (C) Coomassie-stained sodium dodecyl sulfate– polyacrylamide gel electrophoresis gels of purified AIM-A1 variants under nonreducing (left) and reducing (right) conditions. (D) Unfolding temperatures (Tm₅₀) of AIM-A1 variants as determined by the first derivative of thermal shift data (n = 4 independent replicates). Significance was determined via 1-way analysis of variance with post hoc Tukey test correction compared with WT, where ∗∗∗∗P < .0001.