Fig. 11 | Scientific Reports

Fig. 11

From: Chemical finger-printing, antioxidant activity and in silico validation of phytometabolites of Octhochloa compressa

Fig. 11

RMSF profile of NOX (2CDU) protein. RMSF analysis revealed low residue fluctuations (~ 0.05–0.2 nm), indicating a stable protein core, with higher flexibility (~ 0.4–0.45 nm) confined to loop and terminal regions, confirming structural stability across both simulations at 1 ns (A) and 10 ns (B). Radius of gyration profile of NOX (2CDU) protein at 1 ns (C) and 10 ns (D). The Rg values fluctuated slightly between 2.38–2.46 nm throughout both simulations, with consistent RgX, RgY and RgZ components. These results indicate that the protein maintained structural compactness and stability without any signs of unfolding during the simulation.

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