The 9-methyl group of retinal is crucial for the photoreaction of rhodopsin. On the basis of the results of QM/MM simulations, we propose that the primary function of the methyl group is not to properly align the chromophore in the ground state, but that it is a prerequisite for the peculiarly twisted and strained chromophore observed in the batho state. With the methyl group firmly anchored in the protein binding pocket the protein, at the cost of the incipient photon energy, manages to increase the strain energy stored in the chromophore by 25%, which may be crucial for driving the subsequent transformations.
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