contrast the characteristics and functions of myoglobin versus hemoglobin.  1. why are the affinity differences important for the role that these two proteins play?

5. Intravenous solutions must be prepared, to that they are isotonic to red blood cells. A0.9% salt solution is isotonic to red blood cells. Keeping this in mind, explain whatwould happen to a red blood cell placed into a solution of 99.3% water and 0.7% salt.Note to obtain full marks you must care both the intercellular environment to theextracellular environment (solute vs solvent).

The hemoglobin protein has quaternary structure. This means that hemoglobin Selected answer will be automatically saved. For keyboard navigation, press up/down arrow keys to select an answer. a b C P e is composed of subunits binds to the surface of membranes forms part of the quadruple complex changes over time has four-fold symmetry

How does hemoglobin bind O2 cooperatively? A. The binding of one molecule of O2 to one subunit of hemoglobin enhances the assembly of other subunits to form a complete hemoglobin protein. B. The binding of one molecule of O2 to one hemoglobin protein enhances the binding of a molecule of O2 to a different hemoglobin protein. C. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of the same subunit for more molecules of O2. D. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of other subunits for O2.