Flexibility of proteins has been well observed and a role of such dynamics in protein functions seems inevitable. My research interest is the relationship between the dynamic and structural properties of proteins and the function of proteins. The study will be performed on the bacterial heterodimeric enzyme complex imidazole glycerol phosphate (IGP) synthase, a key metabolic enzyme which links amino acid and nucleotide biosynthesis. Biochemical and x-ray crystallographic studies indicate a tight coupling between the two reactions in distinct active sites, suggesting a dynamical role in function. Nonetheless, the details on the exact mechanism regarding the allosteric interactions are still unknown, and that is my very motivation to investigate the dynamics of this enzyme complex. NMR enables non-perturbing measurement of the residue- by-residue dynamics. Comparison of IGP synthase motion alone and substrate(s) or substrate analogue(s)-enzyme complexes will enable characterization of structural and dynamical contributions to function. The study will be carried out by combining NMR structural and spin-relaxation measurements with biochemical characterization of IGP synthase activity. [unreadable] [unreadable]