No abstract

No abstract

With the world turning its attention towards sustainable protein sources, mung bean, in recent times has garnered significant research acclaim. As an emerging functional food that is rich in protein, little is known about its characteristics during processing. Hence, in this study, an molecular dynamic (MD) simulation approach was performed on 2CV6, the crystal structure of 8Sα globulin. GROMACS software was used to vary input thermal and pressure parameters (i.e., 300, 373, and 398 K at 3, 5, and 7 Kbar). Visual MD interface was used to picture the changes occurring in the protein's secondary structure as an effect of applied stress. The radius of gyration values decreased significantly with increasing pressure while high‐pressure high‐temperature treatment improved packing effects. STRIDE analysis showed that peripheral 2° structures such as α‐helices and β‐sheets underwent conformational changes to form turns and coils, indicating increased randomness. Despite subjecting the protein molecule to high temperature, the pressure applied counteracted the unwinding process, resulting in overall compaction.