a. The concerted model can explain well the cooperative binding of oxygen to hemoglobin. Drawthis model below, with a subunit of hemoglobin in the T state as a square and a subunit in theR state as a circle. Include equilibrium arrows between the different states.b. Describe how this model does explain the cooperative binding interaction betweenhemoglobin and oxygen. (in your answer you must make clear why this interaction iscooperative, it is not needed to support this with structural details, e.g. hydrogen bondsspecific conformational changes etc, just use the info in the model)

a. As a text-based AI, I'm unable to draw pictures. However, I can describe how to draw the concerted model.

1. Draw four squares in a row to represent the T state of the hemoglobin subunits.
2. Draw four circles in a row next to the squares to represent the R state of the hemoglobin subunits.
3. Draw equilibrium arrows between the squares and circles to represent the transition between the T state and R state.

b. The concerted model explains the cooperative binding interaction between hemoglobin and oxygen as follows:

In the T state, hemoglobin has a low affinity for oxygen, meaning it does not bind oxygen well. However, when one oxygen molecule binds to a hemoglobin subunit, it causes a conformational change in the entire molecule, shifting it from the T state to the R state.

In the R state, hemoglobin has a high affinity for oxygen, meaning it binds oxygen well. This change in the entire molecule increases the probability of other oxygen molecules binding to the remaining unoccupied subunits.

This is why the interaction is cooperative - the binding of one oxygen molecule increases the likelihood of other oxygen molecules binding. The equilibrium arrows in the model represent this shift from low to high affinity states.