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Analyzing ligand binding to the new and growing group of hemoglobins which are hexacoordinate in the unligated, ferrous state.<br />Most direct measurements of ligand binding exploit lasers or other flashed light sources to initiate the reaction by photolysing the protein-ligand bond for a period of time long enough for the ligand to diffuse out of the protein matrix. When the light pulse is turned off, rebinding can be monitored on time scales much more rapid than those observed in stopped flow mixing. In most cases, these reactions are carried out under pseudo first order conditions with the ligand in excess, resulting in single exponential time courses associated with ligand rebinding to the five coordinate ferrous, unligated (deoxy) hemoglobin.