The article reviews the current status and validation of the AMOEBA polarizable force field, a leading example of the next generation of theoretical models in molecular simulation. The AMOEBA force field is designed to improve upon traditional fixed charge models by incorporating more intricate and accurate descriptions of molecular properties, particularly for small molecules and biomolecules. The authors highlight the field's ability to accurately reproduce molecular polarizabilities and electrostatic potentials, which are crucial for understanding protein-ligand binding and computational X-ray crystallography. They also discuss the field's performance in various applications, including gas phase properties, aqueous peptide solvation, solvation free energies, and protein-ligand binding. The article emphasizes the importance of AMOEBA's consistent treatment of intra- and intermolecular polarization, achieved through a physically motivated damping scheme. Additionally, the authors present validation studies against electronic structure calculations, demonstrating that AMOEBA provides good agreement with benchmark results for conformational energies and nanosolvation properties. The article concludes by discussing the field's performance in predicting solvation free energies for drug-like molecules and its ability to accurately model the dynamics of water near chemically heterogeneous protein surfaces.The article reviews the current status and validation of the AMOEBA polarizable force field, a leading example of the next generation of theoretical models in molecular simulation. The AMOEBA force field is designed to improve upon traditional fixed charge models by incorporating more intricate and accurate descriptions of molecular properties, particularly for small molecules and biomolecules. The authors highlight the field's ability to accurately reproduce molecular polarizabilities and electrostatic potentials, which are crucial for understanding protein-ligand binding and computational X-ray crystallography. They also discuss the field's performance in various applications, including gas phase properties, aqueous peptide solvation, solvation free energies, and protein-ligand binding. The article emphasizes the importance of AMOEBA's consistent treatment of intra- and intermolecular polarization, achieved through a physically motivated damping scheme. Additionally, the authors present validation studies against electronic structure calculations, demonstrating that AMOEBA provides good agreement with benchmark results for conformational energies and nanosolvation properties. The article concludes by discussing the field's performance in predicting solvation free energies for drug-like molecules and its ability to accurately model the dynamics of water near chemically heterogeneous protein surfaces.