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Fig. 2. ITC characterization of Ribose-5-phosphate, Ribulose-5-phosphate and Arabinose-5-phosphate binding to RpiA.Injections were made at rate of 0.5 µl/s and at intervals of 180 s. The first injection peakwas discarded from the isotherm. Areas under thermogrampeaks were calculated and fit toa one-site binding model using Origin (Figure 2) [4].Fig. 3. Binding site of RpiA (ribose-5-phosphate depicted in black).ConclusionsAccording to AUC experiment results Ribose-5phosphate isomerase A is a stable dimer.ITC experiments confirmed that ribose-5-phosphate bind to the active site of protein,however lower affinity was observed for other sugars such as arabinose-5-phosphate andribulose-5-phosphate. Crystal structure of protein complex (RpiA+R5P) should allow us todetermine a mechanism of interaction between protein molecule (RpiA) and ligandmolecule (R5P) (Figure 3).Reference1. Zhang, R., Andersson, C.E., Savchenko, A., Skarina, T., Evdokimova, E., Beasley, S., Arrowsmith,C.H., Edwards, A.M. Structure 11 (1), 31-42 (2003).2. Kim, T.G., Kwon, T.H., Min, K., Dong, M.S., Park, Y.I., Ban, C. Mol. Cells. 27 (1), 99-103 (2009).3. Behike, J., Ristau, O. Biophysical Journal 72, 428-434 (1997).4. Demers, J.P., Mittermaier, A. J. Am. Chem. Soc. 131, 4355-4367 (2009).557