Fig. 7

Analysis of the model of GPAA1^Zn truncated in the same way as the deletion mutant protein yGAA1^70–247 from Saw et al. [16]. a At the left side of panel A, we show the model of the truncated structure (coloured) at the background of the full-length GPAA1^Zn model (grey). At the right side, we present a diagram illustrating and comparing the spatial fluctuations of residues during a molecular dynamics simulation for the truncated (grey) and the full-length (black) GPAA1^Zn model structure. Notably, the α/β fold remained stable along the MD trajectory. The linker (residues 226–239 in accordance with residue numbering in the GPAA1^Zn model) highlighted with a dashed circle that shows larger fluctuation compared to the corresponding region in the full length GPAA1 structure may allow more flexibility at the C-terminus of the truncated GPAA1. b The hydrophobic core was found buried in the truncated model, demonstrating that the truncated GPAA1 could avoid aggregating as it was observed experimentally by Saw et al. [16]