Both myoglobin and Hemoglobin contain a heme prosthetic group with a atom in the center. Unlike hemoglobin, which is comprised of both alpha and beta globin polypeptides, myoglobin is a monomer, thus is lacks structure.

Both myoglobin and Hemoglobin contain a heme prosthetic group with a Iron atom in the center. Unlike hemoglobin, which is comprised of both alpha and beta globin polypeptides, myoglobin is a monomer, thus is lacks Quaternary structure.

Explanation:

The Heme group provides the ability to connect oxygen to myoglobin and hemoglobin due to the existence of an iron atom. It also corresponds to the red color contained in blood and muscles. That faction of hemes includes an iron atom, which can bind to one molecule of oxygen.

Myoglobin is a monomer therefore it has no quaternary structure at all. Myoglobin binds more strongly to oxygen than hemoglobin does. The variation in binding energy represents the transfer of oxygen from the bloodstream, from hemoglobin to myoglobin, into cells.

✿   this landform has a high elevation and a high relief

✿   this landform is a mountain

water is a polar molecule. a chemical bond is a force of attraction between atoms or ions. bonds form when atoms share or transfer valence electrons. atoms form chemical bonds to achieve a full outer energy level, which is the most stable arrangement of electrons. so, false

explanation:

in h2o molecule, two water molecules are bonded by a hydrogen bond but the bond between two h - o bonds within a water molecule are covalent. the greater the electronegativity difference, the more ionic the bond is. bonds that are partly ionic are called polar covalent bonds. nonpolar covalent bonds, with equal sharing of the bond electrons, arise when the electronegativities of the two atoms are equal.