Abstract
The effects of aromatic amino acid residues upon the spectral shift of retinal proteins are investigated by perturbation calculations. The calculated results indicate that phenylalanine, tyrosine and tryptophan can contribute to the opsin shift maximally by several hundred wavenumbers. The results also indicate that the sign and magnitude of the shifts caused by these aromatic amino acid residues depend on mutual configurations between the residues and the retinal. The phenylalanine residue located near the ionone ring induces bathochromic or hypsochromic shifts if the aromatic plane is parallel or vertical to the retinal plane, respectively; the residue located near the Schiff-base induces hypsochromic or bathochromic shifts if the aromatic plane is parallel or vertical to the retinal plane, respectively. The calculated results can explain the experimental results for mutagenesis pigments.
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