Rao S C, Rao C M, Balasubramanian D
Centre for Cellular and Molecular Biology, Hyderabad, India.
Photochem Photobiol. 1990 Mar;51(3):357-62. doi: 10.1111/j.1751-1097.1990.tb01722.x.
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.
我们研究了蜂毒肽和β-乳球蛋白这两种蛋白质处于有序构象和无规卷曲状态时，其色氨酸残基的需氧光解情况。结果表明，蛋白质的构象状态是影响其组成色氨酸残基光解的一个因素。这一点似乎与晶状体蛋白（crystallins）中色氨酸残基的光氧化有关。
