The study focused on how changing the surface-charged residue Asp60 to Lys in myoglobin affects its structural stability when interacting with hydrogen peroxide (H2O2).
Using techniques like UV-Vis absorption and fluorescence spectroscopy, researchers observed significant differences between the wild type myoglobin (Mb(WT)) and the mutant (Mb(D60K)).
The results indicated that Mb(D60K) demonstrated improved structural stability and was less affected by H2O2 compared to Mb(WT), despite only one amino acid being altered.