THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

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Abstract
Abstract— We have studied the aerobic photolysis of the tryptophan residues of the proteins melittin and p‐lactoglobulin when the proteins are in ordered conformations and when they are in randomly coiled states. The results suggest that the conformational status of the protein is a factor that influences the photolysis of the constituent tryptophan residues. This point appears to be of relevance to the photo‐oxidation of the tryptophan residues of the eye lens proteins crystallins.