JMS/sandbox12

Myoglobin was the first solved protein structure and continues to be a classic in protein structure research, which has revealed much about protein dynamics, where myoglobin the protein breaths, if you will, as it changed conformations to take up oxygen and release it, in molecular imitation of our lungs movement. The was solved by John Kendrew in the mid-1900s. Myoglobin is a relatively small protein at 153(sometimes 154) amino acids, and immidiately one appreciates how the polypeptide , cradling it between halves of the protein chain.

Now, in a fascinating article^[1], a team of researchers illuminate how behavior of animals across evolutionary time has been influenced by this . The researchers demonstrate that across the animal kingdom, aquatic animals have myoglobin protein with a great net positive charge than terrestrial animals. The calculate that for every increase in one positive net charge, the animal can accumulate a incredible additional ten times the amount of myoglobin in its cells (muscle cells, in fact), and for two more positive amino acids, the animal can actually accumulate 100 times more myoglobin. More myoglobin translates to more oxygen, which allows aquatic animals to hold their breath for long periods during dives underwater. While the exact mechanism is a fascinating area of ongoing research, it is apparent that myoglobin protein with a greater net positive charge remain soluble at much higher concentrations.

Here we see the whale and elephant myoglobin proteins aligned, with the elephant's amino acids in yellow halos. Without these divergent amino acids, the whole protein has a net charge. After summing the divergent amino acids in whales and elephant, where positive amino acids in blue have a charge value of +1, negative in red of -1, and histidine of +1/2, you'll see that whales overall have a net charge of +3.5, while elephants have only +1. Follow the protein from the beginning of the polypeptide chain until the end yourself, remembering that .

Whether this effect is do to the overall charge of the protein, in repelling two strongly positive proteins; or, whether it is a more local effect, where two proteins cannot interact without unfavarobaly burying the positively charged amino acids; or whether the interactions between myoglobin and the other molecules in the cell, somehow affects its potential to bind to other myoglobins, again, awaits theoretical and experimental insight.

excellent myoglobin tutorial to complement proteopedia articles