Ali Rashidnia - Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Ali Akbar Saboury - Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Reza Rofougaran - Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

Ribonucleotide Reductase (RNR) catalyzes the synthesis of the four deoxyribonucleotides needed for DNA synthesis and repair in cell. The RNR protein consists of two non-identical subunits, the R۱ and R۲ proteins. The latter protein contains an iron-tyrosyl free radical center essential for enzyme activity. This enzyme has been targeted for cancer treatment. Therefore, structural studies on this enzyme has important role for designing of new antimetabolites. Under physiological conditions, this protein has a high Į-helical content. It is important to know how structure of RNR folds into their biologically active states and how these active states are stabilized.[۱,۲].

Ribonucleotide Reductase (RNR), Stability, Circular dichroism