Running computational simulations to visualize how G6PD mutations affect protein stability and dynamics at the atomic level.
Root Mean Square Deviation (RMSD) measures how much the protein structure deviates from its starting configuration. Higher values indicate instability.
Hydrogen bonds are critical for protein stability. The S188F mutation disrupts key bonds at the dimer interface.
Mediterranean variant (S188F) shows significantly higher structural deviation over 100ns, indicating reduced stability compared to wild-type enzyme.
The S188F mutation breaks critical hydrogen bonds at the dimer interface, weakening the quaternary structure essential for enzyme function.
Class I mutations show increased flexibility in the NADP+ binding pocket, reducing cofactor affinity critical for enzyme stability.
RMSF analysis reveals increased flexibility in catalytically important regions (residues 180-200) in mutant structures.
Continue exploring our computational approaches to G6PD research.