Extending MMPBSA for membrane proteins: Addressing P2Y₁₂R conformational changes upon ligand binding.

ABSTRACT: Membrane proteins play crucial roles in biological signaling and represent key targets in drug discovery, garnering significant experimental and computational attention. Recent advances in computational screening techniques have enabled the development of more accurate and efficient binding affinity calculation methods. Among these, the molecular mechanics Poisson-Boltzmann surface area (MMPBSA) method has gained widespread adoption in large-scale simulations due to its computational efficiency. However, its application to membrane protein-ligand systems remains less developed compared with globular protein systems, primarily due to the additional complexity introduced by the membrane environment. In this study, we present enhanced capabilities in Amber that provide flexible and automatic

SUBMITTER: Zhao C 

PROVIDER: S-EPMC12574936 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature