The document analyzes the D30N/L90M dual mutation in HIV-1 protease that confers drug resistance. Molecular dynamics simulations were performed on the wild type, D30N, and D30N/L90M variants. Dynamic residue interaction network (dRIN) analysis found that the dual mutation greatly reduced hydrogen bonding between residues near the dimer interface and increased a van der Waals interaction between residue 90M and 25D. This disrupts dimer formation in protease conformational changes, explaining why the dual mutation is rarely observed in vivo.