What Are The Structural-Molecular Hydrochemistry Changes That Occur In Hemoglobin

(a) Describe THREE types of chemical bonds/interactions found in proteins. For each type, describe its role in determining protein structure.

Haemoglobin is just one of the many possible forms and functions of a protein polymer. They all have different structures, which makes them specialised to carry out a particular function. For example enzymes. They are roughly spherical in shape due to the tight folding of the polypeptide chains. Enzymes play important roles in most biological processes, in particular metabolism and synthesis. The tertiary structure of an enzyme is of particular importance to its function and a slight change in the chain sequence and therefore it's shape can result in it becoming inactive. Enzymes work by combining with a substrate to form an enzyme-substrate complex, the substrate is then broken down and released. Each enzyme has a particular substrate that is can breakdown, this will be the substrate with the complimentary structure to that of the active site of the enzyme. For example starch is only broken down by amylase. As the shape of the active site depends on the shape of the polymer shape so does the over all function of the enzyme.

Hydrogen bonds contribute to a property of water called cohesion or the tendency of water molecules to stick together.

29. If all the 280 million molecules of hemoglobin contained in RBCs were free in the plasma,

2. Which of the following terms refers to either a reduction in the quantity of hemoglobin or a reduction in the volume of red blood cells?

J.) As Cari’s Pco2 and alkaline blood pH rose, how was the oxygen-carrying capacity of hemoglobin affected?

Hydrophobic molecules don’t like water, which means they will propel away from water. Hydrophilic molecules

Hemoglobin can bind to four molecules of oxygen. When a hemoglobin molecule binds to oxygen molecules, the resulting molecule is referred to as oxygenated hemoglobin. Hemoglobin molecules that are not bound to any oxygen molecules are referred to as deoxygenated hemoglobin (Harvey, et al., 2011). Oxygenated hemoglobin is formed through the transportation of oxygen to cells in tissues.

Haemoglobin is a water soluble quaternary structured globular protein made up 4 chains of amino acids, 2 alpha and 2 beta subunits and are all attached to an inorganic prosthetic group (Fe2+) known as ‘haem’. The ring of carbon atoms are attached to the haem embedded into the centre,

Yes, the change of the amino acid in the protein influences the overall structure. The healthy hemoglobin looks fairly spherical, with a few lumps on the surface. The Sickle Cell Anemia Hemoglobin looks like two identical, bumpy spheres were glued together to form one shape.

Hemoglobin is present in red blood cells of the body and transport oxygen from lungs to the rest of the human body (National, 2015). Humans carry different types of hemoglobin, but there are three common types found in the gel electrophoresis. One of the test blood that help people to diagnose any disease is the hemoglobin electrophoresis. Hemoglobin electrophoresis test looks at the different types of hemoglobin in the blood, and can help diagnose the type of anemia that the person could have (National, 2014). The three common types of hemoglobin presents in humans are normal hemoglobin, sickle trait hemoglobin, and sickle cell hemoglobin. Abnormal hemoglobin, called hemoglobin S, causes sickle cell disease (SCD). The sickle cell hemoglobin

In order for haemoglobin to be made from the base sequence provided, protein sysnthesis needs to occur. Consequently, two major events are involved; transcription, which makes messenger RNA (mRNA) that holds the codons that tRNA will translate into amino acids and eventually a polypeptide; and transcription, which makes polypetide chains that make proteins. In relation the hameglobin structure, the DNA (base sequence provided) partially unwinds, so it can be read. RNA polymerase enzymes attach onto the promoter reigon of the gene. The RNA polymerase assists in the complementray base pairing of free ribonucleotides with exposed bases of the template strand of DNA. Therefore, new hyrdogen bonds will be formed between the bases of DNA and the newly formed RNA molecule. When the RNA polymerase reaches the terminal reigon of the gene, hydrogen bonds break of and a newly formed mRNA strand C A U C U A A C C C C A G A G G A G is created.

The histidine (HIS-18, in view 2) is connected to the iron in the heme also by a covalent bond. In this case, one nitrogen from the histidine residue shares an electron-pair with the iron in the heme. This is an important bond as well. When the heme is bound to oxygen, its conformation

This process disrupts non-covalent bonds, such as ionic, hydrogen and hydrophobic bonds, due to their susceptibility to pressure. HHP does not affect vitamins and aromatic compounds due to their low molecular weight (Carlez, Rosec, Richard, & Cheftel, 1994). In the case of larger molecules, such as proteins, their structure is lengthened after HHP treatment, which in essence destroys the 3D structure of the large molecule, thus changing the structure of a protein or in the case of enzymes,

Meanwhile, if temperature is increased denatures the proteins. Proteins then unfold and the non-polar groups which were previously in the interior of the molecule become exposed. This leads to a decrease in the solubility of the protein in aqueous environment. Addition of ethanol, methanol, acetone and the like decreases the dielectric constant and thus decreases protein’s solubility. (Boyer, 2000)