what type of secondary structure dominates the conformation

Solution

Hemoglobin is composed of four monomers.There are two alpha chains,each with 141 amino acids,and two beta chains,each with 146 amino acids.There are two states in the hemoglobin,the T state and the R state.The T state has a less of an affinity for oxygen than the R state.The hemoglobin must either be in its T state or R state.The conformation state of the monomer changes as it binds to oxygen.The conformation of hemoglobin also changes as the oxygen binds to the iron,raising both the iron and the histidine residue bound to it.When a monomer of hemoglobin binds to oxygen,it alerts other nearby hemoglobin monomers to start the binding process as well.This means that,as more and more oxygen is bound by hemoglobin monomers,the affinity of hemoglobin will increase more and more as well.The affinity of hemoglobin is proportional to the quantity of oxygen bound at a given time.This allows hemoglobin to increase its affinity for oxygen over time,a property that brands it as one of the most flexible proteins in the body.

Hemoglobin is whose secondary structure is dominated by the alpha-helix.Hemoglobin undergoes several conformational changes upon binding with oxygen.As soon as the iron cation within hemoglobin begins to move,the Histidine residues and the alpha-helix of hemoglobin start moving as well to stabilize the changes caused by the movement of iron.Then the carboxyl terminal end of the alpha-helix usually resides at the interface between the two alpha and beta dimers that make up hemoglobin.The positional changes of the carboxyl terminal end create favorable conditions for transitions between the T- and the R-states of hemoglobin.