Question- Muscle contracts by sliding myosin filaments relative to actin filaments. The myosin head group hydrolyzes ATP to get the energy for its globular motor Doman to move a long lever-arm domain. Suzuki et al. (1998) used GFP and its mutated relative blue fluorescent protein (BFP) in a fluorescence resonance energy transfer (FRET) experiment to demonstrate that during the working stroke the lever-arm domain tilts against the motor domain. They constructed a fusion protein in which GFP was attached through three glycines to the N-terminal end of the myosin and BFP was attached in the same way to the C-terminal end. Exciting the BFP causes the GFP to fluoresce with an efficiency of 0.333 after the ATP is hydrolyzed to ADP, and this corresponds to a distance of 3.8 nm. Before the hydrolysis, the FRET efficiency is 0.082. How far do the two fluorophores move relative to each other during the working stroke?
Provide your answer in scientific notation