Abstract
The dynamic nature of protein structure is widely accepted [1, 2]. Careful studies of room temperature tryptophan phosphorescence (RTTP) lifetime provides an information on the rigidity of the emitting tryptophan environment. [3, 4]. Earlier we have demonstrated glycogen phosphorylase b (EC 2.4.1.1) to exhibit long lived RTTP [5]. This paper presents the phosphorescence technique application to the study of internal dynamics of glycogen phosphorylase b. The RTTP lifetimes were determined depending on concentration of glucose 1-phosphate (substrate), glucose (competitive inhibitor), after dimer association and temperature aggregation of the enzyme.
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