The conformational status of a protein influences the aerobic photolysis of its tryptophan residues: melittin, β-lactoglobulin and the crystallins

Rao, S. Chenchal ; Rao, Ch. Mohan ; Balasubramanian, D. (1990) The conformational status of a protein influences the aerobic photolysis of its tryptophan residues: melittin, β-lactoglobulin and the crystallins Photochemistry and Photobiology, 51 (3). pp. 357-362. ISSN 0031-8655

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1751-...

Related URL: http://dx.doi.org/10.1111/j.1751-1097.1990.tb01722.x

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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