To take the percent by mass of this element, we use the
formula:
% mass = (mass of element / mass of ore) * 100%
% mass = (47.5 g / (660 kg * 1000 g / kg)) * 100*
<span>% mass = 7.20 x 10^-3 %</span>
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 hydrophobic effect is caused by nonpolar molecules clumping together. Large macromolecules can have hydrophobic sections, which will fold the molecule so they can be close to each other, away from water. Many amino acids in proteins are hydrophobic, helping the proteins obtain their complicated shapes. The hydrophobic effect extends to organisms, as many hydrophobic molecules on the surface of an organisms help them regulate the amount of water and nutrients in their systems.
Answer:
6 is the right answer I know cause I like science
