Primary Structure: This is hemoglobin at its simplest level, it is made up of chains of amino acids, where 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 custom-made essay on “Why Violent Video Games Shouldn't Be Banned”? Download an Original Essay Secondary Structure: The two types of secondary structure found in proteins are Alpha-Helix (?) or Beta-Pleated Sheet ( ?) . Both of these structures 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 folding of hemoglobin, creating the 3D structure of the chain. Hemoglobin is a globular protein, which means that spherical structures are formed, where the hydrophobic part is towards the center and the hydrophilic part is towards the edges, which means that they are soluble in water.Quaternary structure: They are proteins that contain more than one polypeptide chain held together by hydrogen, ionic, and disulfide bonds. Hemoglobin has four polypeptide chains and all contain a heme group. Additionally, there is 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 within 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 non-polar side chains, meaning they are uncharged. Hydrophilic Interaction – Found on the outside of the 3D structure of hemoglobin. They are hydrophilic, which means 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 that are located on two opposite cysteine ​​amino acids. When this happens, everyone loses an H?. These are exceptionally strong bonds and can only be broken by reducing agents, not by things like pH temperature. Hydrogen bonds: can form between an oxygen or nitrogen atom and a hydrogen atom present on several amino acids. For this to happen, the oxygen or nitrogen must have a lone pair of electrons to form a hydrogen bond. So, a pair of electrons will be shared by the nitrogen or oxygen atom on an amino acid and by the hydrogen atom on the amino acid. Ionic bonds – Form between oppositely charged variable (R) groups that contain a carboxylic acid (-COOH) and an amino group (-NH2). These bonds are stronger than hydrogen bonds, however they can be broken by a change in temperature or pH. Please note: this is just an example. Get a custom paper from our expert writers now. Get a Custom Essay The Function of Hemoglobin: Hemoglobin is found in red blood cells, where it carries oxygen through the respiratory system and into the rest of the body. It is a globular protein that displays a quaternary structure and also contains other structures such as heme groups and iron ions. This allows oxygen to bind to it, and this is possible because the iron ion gives hemoglobin a high affinity for oxygen.