Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
The velocity of the gas is inversely proportional to the square root of the molar mass of the gass. Heavier molecules tend to travel slow compared to light molecules. Among these, He has the lowest molar mass of 4 g/mol hence this element has the greatest velocity among all molecules given.
Answer:
they all have the same amount of kinetic energy
A condensation reaction is described to be a reaction wherein two molecules form an even larger product and consequently produces a smaller molecule as a by-product. For example, when two amino acids are combined, a dipeptide bond is formed. As a result, 1 molecule of water is produced as a by-product.
