Myoglobin Structure: Myoglobin is a single-chain globular protein of 153 or 154 amino acids, containing the heme prosthetic group

in the center, The remaining apoprotein folds around this. It is made up of eight alpha helices and a hydrophobic core. Unlike haemoglobin, which myoglobin is structurally similar to, this protein does not show cooperative binding of oxygen. The binding of oxygen to myoglobin is unaffected by the oxygen pressure in the surrounding tissue. Function: Myoglobin is an iron and oxygen and binding protein found in the heart and skeletal muscle tissues of almost all vertebrates and mammals. It is closely linked with hemoglobin. It has oxygen molecules attached to it, so when working at high levels of activity it provides extra oxygen to the active muscles to enable the body to stay active for a longer period of time. Another role of myoglobin is in the repair of damage muscles, stimulating the protein to be released into the bloodstream, This is the only time when myoglobin is found in the blood. When in excess amounts the kidneys aid in its removal from the blood by incorporating it into the urine. However, in large amounts myoglobin can damage the kidneys. The binding similarities of oxygen between myoglobin and hemoglobin provides an important factor of their function. Both of these proteins bind efficiently with oxygen when the concentration of it is very high, for example, in the lungs. However, haemoglobin is much more likely to release this oxygen in areas of low concentration, e.g. in tissues. Haemoglobin binds less compactly than myoglobin does in muscle tissues, this means that haemoglobin is a more effective transport mean of oxygen throughout the body. It is said that myoglobin has a instant binding tenacity t o oxygen given its hyperbolic oxygen dissociation curve. When the concentration of myoglobin is high within muscle cells, it allows the organisms to hold their breath for longer. Myoglobin wouldnt be as effective as a transporter of oxygen, its cooperative binding of oxygen is much tighter than that of haemoglobin and will only release its oxygen in extreme conditions. Myoglobin also has a strong affinity for oxygen which allows it to store the molecule much more effectively. This is an important component in the tissues when the body is starved of oxygen, for example, during high intensity physical activity when carbon dioxide levels and the lactic acid concentration is very high in the muscles. These two factors are what simulate the myoglobin to release its oxygen, as to protect the bodys muscles from damage. The higher the concentration of myoglobin within muscle cells, the longer the endurance of muscle. This is why mammals such as seals and whales have high concentrations of myoglobin in their muscles.

Interesting fact: Myoglobin is one of the most frequently studied proteins in science, but its true physiological function has not been conclusively established yet. One experiment that was conducted to try and determine was that a group of mice were genetically engineered to lack the protein myoglobin. These mice showed a 30% reduction in cardiac systolic out than that of normal mice. They then adapted to deal with this by increasing their vasodilation and genetic mechanisms.