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.
Item Type: | Article |
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Source: | Copyright of this article belongs to American Society for Photobiology. |
ID Code: | 1240 |
Deposited On: | 04 Oct 2010 08:03 |
Last Modified: | 13 May 2011 07:36 |
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