title: The conformational status of a protein influences the aerobic photolysis of its tryptophan residues: melittin, beta-lactoglobulin and the crystallins.
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.
authors.affiliation: Centre for Cellular and Molecular Biology, Hyderabad, India.
authors.forename: S C
authors.initials: SC
authors.lastname: Rao
authors.forename: C M
authors.initials: CM
authors.lastname: Rao
authors.forename: D
authors.initials: D
authors.lastname: Balasubramanian
mesh_terms: D000332:Aerobiosis; D001514:Bee Venoms / Q000528:radiation effects*; D003459:Crystallins / Q000528:radiation effects*; D007782:Lactoglobulins / Q000528:radiation effects*; D008555:Melitten / Q000528:radiation effects*; D010782:Photolysis; D011487:Protein Conformation; D014364:Tryptophan; D014466:Ultraviolet Rays
chemical_list: D001514:Bee Venoms; D003459:Crystallins; D007782:Lactoglobulins; D008555:Melitten; D014364:Tryptophan