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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?

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