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- W2027565614 abstract "We have studied the aerobic photolysis of the tryptophan residues of the proteins melittin and beta-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." @default.
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- W2027565614 date "1990-03-01" @default.
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- W2027565614 title "THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β- LACTOGLOBULIN and THE CRYSTALLINS" @default.
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- W2027565614 doi "https://doi.org/10.1111/j.1751-1097.1990.tb01722.x" @default.
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