GROMACS is a molecular dynamics simulation tool that we use to investigate the conformational dynamics and solvent-mediated stabilization of transthyretin (TTR). Our work focuses on resolving how hydration shapes structural stability and ligand accessibility within the dimeric channel of the tetramer. By combining trajectory analysis of solvent-accessible surface area (SASA), hydrogen-bond networks, and spatially resolved water occupancy, we quantify how solvation reorganizes across the channel depth. Time-resolved analyses of water residence times enable classification of bulk-like “fast” waters, confined “slow” waters, and long-lived structural waters that contribute to kinetic barriers and stabilization of the tetrameric interface. These simulations provide mechanistic insight into how solvent dynamics modulate TTR stability, ligand binding, and channel accessibility, linking microscopic hydration behavior to experimentally observed structural and thermodynamic properties.