This molecule fluctuates between T and R states.
One model that explains the allosteric change in this protein is the Monod, Wyman, and Changeux model. The Koshland, Nemethy, and Filmer model states that one subunit's change in the structure of this protein promotes conformotional state changes in adjacent subunits. This molecule fluctuates between T and R states. 2,3-bi-phospho-glycerate and inositol hexa-phosphate act to promote the disassociation between this protein and the molecule that it most commonly binds to. The fact that the aforementioned disassociation is promoted when this protein is at low pHs is called the Bohr effect. The carbamation of its N-terminal amino groups allows this protein to carry carbon dioxide. For 10 points, name this iron-containing protein found in red blood cells, responsible for carrying oxygen.
One model that explains the allosteric change in this protein is the Monod, Wyman, and Changeux model.
 hemoglobin [accept Hb; or Hgb]