And by stabilizing the T state, that drives the equilibrium back towards the T state. And now the T state can exist by itself without binding to that oxygen. And what that means is that basically shifts the entire curve toward the right side and then decreases the affinity of the hemoglobin for oxygen because now the T state can exist because it is more stable than in the absence of that 23 BPG. So once again, the T state of hemoglobin in its pure form is highly unstable because it contains a pocket with positive charges at the center of that tetrimer where the positive charges come from these six amino acids found on these opposing beta subunits. So this instability pushes the equilibrium towards the R state, towards the right side. And physiologically, what this means is pure hemoglobin, in the absence of two three BPG would bind oxygen way too strongly with a very high affinity because it would exist predominantly in the R state.