Palmitoylation at the N-terminal disordered region of PSD95 acts as a conformation switch and facilitates PSD95 cluster formation on synaptic membrane: Molecular insights from multiscale simulations

This dataset contains trajectory and coordinate files used in the molecular dynamics simulations reported in our study on the role of palmitoylation in PSD95 clustering. The simulations, conducted using all-atom and coarse-grained approaches, explore how palmitoylation influences the conformation and membrane association of PSD95, a key postsynaptic scaffolding protein. These data support our findings that palmitoylation promotes extended conformations and domain rearrangements that are critical for PSD95 cluster formation and synaptic organization. We have also included a powerpoint file where all the trajectory movie files (supporting information) are available.