THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β- LACTOGLOBULIN and THE CRYSTALLINS (original) (raw)

Photochemistry and Photobiology, 1990

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.

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