HandyFRET is the set of three simple computational methods that can potentially replace MD simulations in FRET data interpretation. The main hurdle in such analysis is the dependency of energy transfer on the diffusion of the dyes about the point to which they are tethered and the relative orientation of the dyes. Using the simple methods you can:

• Assess how the shape of protein can restrain the free rotation of the dyes and how it affects the final shape of FRET efficiency distribution.
• Reveal the differencies between the static and dynamic averaging regimes of the transfer efficiency.
• Check how much of broadening of the FRET efficiency distribution comes from the dye diffusion and how much comes from dynamics of the host macromolecule.
• Assess the shift between the average distance between dyes and the actual distance between macromolecule residues to which they are attached.
• Quickly test if the given protein model is consistent with experiments.

The three methods are described in the tabs above, with the Avaliable volume approach being the quickest to run and the Snapshot library being the most detailed.

HandyFRET is developed in the Corry Research Group at the Australian National University.