3.5.2. Radius of Gyration (Rg) and Solvent-Accessible Surface Area of Protein (SASA)

Radius of gyration (Rg) is measure of protein compactness, stability, integrity and foldness of protein backbone. The Rg trajectory for NEK7 is depicted in Figure 14. Trajectory analysis for the radius of gyration revealed that protein retained compactness throughout the simulated trajectory, and only slight fluctuations were observed around 30 ns, which stabilized after a short period of time.

**Figure 14.** Radius of gyration (NEK7).

Solvent-accessible surface area (SASA) is the area of protein that is accessible by the solvent. The higher the value for SASA, the lower the stability of the protein. In the current study, residue wise SASA was calculated and ranged between 180 to 350 Å<sup>2</sup> , which is quite acceptable. The average SASA value was computed to be 282.72 Å<sup>2</sup> (Table 5). The residue wise SASA of targeted protein is shown in Figure 15.
