The original approach was developed for the modelling of large conformational changes in proteins . This approach was built on the Martini 2 by replacing the harmonic bonds from Elnedyn approach with LJ potentials between backbone (BB) CG beads, and here denoted as GōMartini 2. These LJ interactions are defined using a native contact map (NCM), which serves as a guide for preserving protein structure. The NCP is generated using residue overlap (OV) and restricted chemical structural units (rCSU) methodologies. OV is based on the van der Waals radii of heavy atoms. It determines contacts by calculating the overlap of spherical representation of these atoms. To account for attractive interactions, the radii are scaled by a factor of 1.24 . The rCSU method incorporates attractive and repulsive electrostatic forces, considering hydrophobic, hydrophilic, and aromatic interactions. A contact is established if the attractive forces outweigh the repulsive ones . The parameter 𝜎 𝑖 𝑗 is calculated as 𝑑/2 1/6 , where 𝑑 represents the C𝛼-C𝛼 distance between a contact pair. The parameter 𝜖 𝑖 𝑗 , which accounts for hydrogen bonds, ionic bridges, and hydrophobic interactions, is set to a fixed value of 9.414 kJ/mol. The GōMartini 2 approach demonstrated excellent performance in various applications from the catalytic pocket motions in the Man5B enzyme (in agreement with AA-MD), nanomechanics of titin domain and mechanical failure of fibrils of self-assembling peptides . Additionally, this method enabled the folding of both 𝛼-helices and 𝛽-hairpins, achieving timescales comparable to experimental observations .