Explanation:
Haemoglobin consists of heme unit which is comprised of an <u>
</u> and porphyrin ring. The ring has four pyrrole molecules which are linked to the iron ion. In oxyhaemoglobin, the iron has coordinates with four nitrogen atoms and one to the F8 histidine residue and the sixth one to the oxygen. In deoxyhaemoglobin, the ion is displaced out of the ring by 0.4 Å.
The prosthetic group of hemoglobin and myoglobin is - <u>Heme</u>
The organic ring component of heme is - <u>Porphyrin</u>
Under normal conditions, the central atom of heme is - <u></u>
In <u>deoxyhemoglobin</u> , the central iron atom is displaced 0.4 Å out of the plane of the porphyrin ring system.
The central atom has <u>six</u> bonds: <u>four</u> to nitrogen atoms in the porphyrin, one to a <u>histidine</u> residue, and one to oxygen.
It would be most similar to neon. it wouldn’t be sulfur because that’s in the same group as oxygen and has the same number of electrons. and carbon has less than that so the only one that makes sense is neon
The peptide given above is made up of the following amino acids: glycine [G], leucine [L], valine [V], isoleucine [I] and tryptophan [W]. These amino acids are joined together by amide bond to form peptide. Peptides usually have two terminals, the N terminal and the C terminal. For GLVIW, the C terminal end amino acid is tryptophan, that is the last amino acid on the peptide chain. The N terminal amino acid is glycine, that is, the first amino acid on the peptide chain.
