True or False: The binding of oxygen to hemoglobin changes its structure.

The statement that the binding of oxygen to hemoglobin changes its structure is true. When oxygen molecules bind to hemoglobin, they induce a conformational change in the protein's structure. This change is often described as a switch from a tense (T) state to a relaxed (R) state, which enhances the ability of hemoglobin to bind additional oxygen molecules.

This phenomenon is a key aspect of hemoglobin's quaternary structure, which allows it to effectively transport oxygen from the lungs to tissues throughout the body. As more oxygen binds to hemoglobin, the structural changes increase its affinity for additional oxygen, facilitating efficient oxygen uptake in the lungs and release in the tissues where it's needed.

This cooperative binding is crucial for the functionality of hemoglobin, as it allows for a more responsive reaction to varying oxygen levels in different physiological conditions.