DEPENDENCE OF PROLONGED AFTERLUMINESCENCE OF PROTEINS ON THE SECONDARY STRUCTURE OF THEIR MOLECULES

Investigations were made of the parameters of a number of proteins in a native state, in solutions of urea, guanidine dodecylsulfate, and in weakly polar solvents. Unfolding of the secondary structure of macromolecules of protein is accompanied by an increase in the constant of rate of attenuation and a lessening of intensity of luminescence. An increase, under the influence of dodecylsulfate, of the degree of spiralization of protein which has been denatured by urea leads to restoration of the value of K to values which are characteristic for native protein. An increase of degree of spiralization with a simultaneous disruption of tertiary structure leads to an increase in intensity and decrease of the constant of the rate of attenuation of after-luminescence. The structure of a macromolecule exerts a predominant influence on the parameters of afterluminescence of proteins in the course of obscure processes which begin after cessation of irradiation and lead to scintillation.
Trans. of Biofizika (USSR) v13 n3 p428-432 1968.