Primary structure: This is hemoglobin at the simplest level, it is made up of chains of amino acids, in which peptide bonds separate each amino acid. It consists of four polypeptide chains, two alpha (?) chains and two beta (?) chains. Say no to plagiarism. Get a tailor-made essay on “Why violent video games should not be banned”?Get the original essaySecondary structure: The two types of secondary structure found in proteins are the alpha helix (?) or the beta pleated sheet ( ?). These structures both involve polypeptide chains, however, in this case they form different shapes, these are held together by weak intermolecular forces called hydrogen bonds. Hydrogen bonds can be found between the NH and C=O groups, giving it a more stable structure. Tertiary structure: This is the main bond involved in stabilizing the structure of each hemoglobin chain. The heme molecule is involved in the curvature of hemoglobin, creating the 3D structure of the chain. Hemoglobin is a globular protein, this means that ball-shaped structures are formed, where the hydrophobic part is towards the center and the hydrophilic part towards the edges, this means that they are soluble in water. Quaternary Structure: These are proteins that contain more than one polypeptide chain that is held together by hydrogen, ionic, and disulfide bonds. Hemoglobin has four polypeptide chains, and all contain a heme group. There is also an iron ion (Fe²?), this is where oxygen binds due to iron's high affinity for oxygen. Hemoglobin can be found in red blood cells in the circulatory system. How the protein is able to maintain its structure: Hydrophobic interaction – These weak bonds are found inside the 3D structure of hemoglobin and form between the R groups, which contain only hydrogen and carbon. These interactions are hydrophobic, meaning they repel water. These amino acids contain nonpolar side chains, meaning they are not charged. Hydrophilic interaction – These are found outside the 3D structure of hemoglobin. They are hydrophilic, meaning they attract water. These amino acids contain polar side chains, which means they are charged. Overall, this means that hemoglobin is soluble in water. Disulfide bridges – They form between two sulfur atoms present on two opposing cysteine ​​amino acids. When this happens, everyone loses an H?. These are exceptionally strong bonds and can only be broken by reducing agents, not things like pH temperature. Hydrogen bonds – These can form between an oxygen or nitrogen atom and a hydrogen atom present on different amino acids. For this to happen, the oxygen or nitrogen must have a pair of free electrons in order to form a hydrogen bond. Then, a pair of electrons will be shared by the nitrogen or oxygen atom on an amino acid and the hydrogen atom on the amino acid. Ionic Bonds – These are formed between oppositely charged variable (R) groups that contain a carboxylic acid (-COOH) and an amine group (-NH2). These bonds are stronger than hydrogen bonds, however, they can be broken by a change in temperature or pH. Keep in mind: this is just a sample. Get a personalized article from our expert writers now. Get a Personalized Essay The Function of Hemoglobin: Hemoglobin is found in red blood cells, where it carries oxygen across..