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Site directed spin labeling studies of proteins have emerged over the recent years, in combination with EPR spectroscopy the technique allows the sample to be studies in its natural like environment. The article presents the results of the spin labeled Bos Taurus hemoglobin investigation under different environmental setups. The protein study was carried out to see the motional behavior and the dynamic conformational fluctuations in different viscous solvents, and a molecular crowding investigation was also carries out on the sample in order to obtain a full spectrum of the environmental impact on the spin labeled hemoglobin.

Keywords: hemoglobin, EPR, site directed spin labeling, protein dynamics.