This CG model, rooted in the Shinoda-DeVane-Klein (SDK) framework developed in 2007 for the self-assembly of aqueous surfactant , has evolved through the SPICA CG potential. It was parameterized by fitting thermodynamic properties such as surface tension, density, and transfer free energy. SPICA effectively captures the self-assembly processes of surfactants and lipids with realistic interfacial behavior. Recently, its applications have extended beyond its initial scope to include simulations of lipids and proteins in a polar solution . The SPICA protein model incorporates an elastic network (EN) model to maintain the initial secondary and tertiary structure of a single protein in solution during CG simulations . In this case SPICA+EN model, a harmonic bond is established between two backbone (BB) particles when they are separated by more than two bonds or by a spatial distance of less than 9 Å. As suggested by prior studies, a harmonic spring constant of 1195 kcal/mol/Å 2 is used. Notably, both the cutoff distance and spring constant in the EN model can be adjusted to suit the target system. The application of EN model on top of SPICA model restricts the study of large conformational changes in structured proteins, such as protein unfolding driven by temperature or mechanical forces.