Final answer:
The shape of an oxygen dissociation curve for myoglobin is hyperbolic, while for hemoglobin it is S-shaped. Myoglobin has a higher oxygen affinity than hemoglobin at low oxygen pressures. Hemoglobin exhibits cooperativity and releases oxygen to the tissues at lower oxygen pressures.
Step-by-step explanation:
The shape of an oxygen dissociation curve for myoglobin is a simple hyperbolic curve, whereas for hemoglobin it is S-shaped. Myoglobin has a higher oxygen affinity than hemoglobin at low oxygen pressures, meaning it can bind oxygen more tightly. This allows myoglobin to efficiently extract oxygen from the environment. Hemoglobin, on the other hand, exhibits cooperativity, where the binding of oxygen to one heme group enhances the affinity of the others. This results in hemoglobin releasing oxygen to the tissues when the oxygen pressure is lower.