Simulation data for “Time-resolved fluorescence anisotropy and molecular dynamics analysis of a novel GFP homo-FRET dimer”

In this work, molecular dynamics simulations were carried out to study the dynamical properties of a monomer and a dimer of green fluorescent protein (GFP) in order to provide an in-silico validation of FRET (Förster resonance energy transfer) efficiency, calculated from the fit of the fluorescence anisotropy decays with a stretched exponential decay model. An excellent agreement was found between model and experiments. Dynamical insights on the dimer linker and on the protein tumbling were also obtained from the simulations. The molecular dynamics data are provided here.