Function and Structure of Hemoglobin and Myoglobin Essay

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.

11. Small insects may take a bubble of air underwater when they dive. The bubble can serve as an air tank for some time because

5. Under normal conditions, what is the fate of the globular proteins of a recycled hemoglobin molecule? B they are disassembled into their component amino acids

In the continued process of realizing how much sugar content was in the food and beverages I was consuming and going to the doctor receiving my blood work results, I decided to change my nutritional habits. I went to my primary care provider to get my six-month checkup and was informed that my Hemoglobin A1C levels were high (5.9%). Over the course of the summer/winter break I was consuming too much of sugary food items and beverages while on a cruise as well. I can agree that I consumed large amounts of sugary foods while on my summer break and now this has changed my way of thinking about nutritional sugary content. Whenever I would feel the need to have a snack, I would want something sweet to curve my appetite at the moment.

The structure and colour of a red blood cell is come from the haemoglobin which consists of four folded chains of amino acids, this forms the sub groups which are smaller haem groups that are attached together. For each haem group there is an iron molecules which is in a ferrous state (Fe2+), there is 2 sub unit of Alpha (α) which consists of 141 amino acid and 2 sub unit of Beta (β) which consists of 146 amino acid. The haem group keeps the structure of the haemoglobin in place. When an oxygen (O2+) molecule is carried by the red blood cell, it forms a weak ionic bond with the Fe2+ molecule in the four haem group, this is then transported to the rest of the body. Haemoglobin and oxygen combine to form oxyhaemoglobin, this is the reason the blood cell is bright red, when the oxygen is transported to the region it is needed the blood turns back in to haemoglobin this is where its deoxygenated blood and it returns back to the heart then to the lungs where diffusion occurs (CO2) removed through the capillary wall and O2 is absorbed into the blood). Blood being unable to pick up 02 molecules would mean less oxygen will be able to be transported, which would mean that the heart would have to work much harder to transport the small amount of oxygen in the body, this

The blood protein in Methemoglobinemia are unable to carry oxygen, which makes it harder for the tissue to get the amount of oxygen

Anemia is a condition in which the concentration of red blood cells or hemoglobin in the blood is below normal. Hemoglobin is a substance in red blood cells that carries oxygen to the tissues of the body. Anemia results in not enough oxygen reaching these tissues.

The base mutation of adenine to thymine which results to in substitution of valine for glutamic acid in the sixth residue of the b chain. This mutant hemoglobin is called leading to the presence of hemoglobin S (HbS), instead of HbA in the red blood cells (RBCs) .The presence of hydrophobic valine residue in ß subunits cause small change lead to the polymerisation of deoxygenated HbS monomers into long insoluble multi-stranded fibers of approximate 21.5 nm diameter (8) .

. The 3-D tertiary structure of polypeptide proteins globular and is the result of interactions that occur between R groups. Tertiary structure is a result of the bonds between sidechains of amino acids, the R groups. The structure and bonds involve alpha helices, beta pleated sheets, and also regions unique to each protein. Tertiary proteins are held together by four different types of forces; hydrogen bonds, hydrophobic interactions (including Van der Waals interactions), ionic bonding (electrostatic interactions), and disulfide bridges (strong covalent bonds). Hydrogen bonds occur within and between polypeptide chains and the aqueous environment. Hydrogen bonding forms between a highly electronegative oxygen atom or a nitrogen atom and a hydrogen atom attached to another oxygen atom or a nitrogen atom. This links the amino acid

They are known to be the workhorses of the body cell that carries out diverse catalytic and structural roles into building the structures of all living organisms [15]. The basic structure of protein is a chain of amino acids that supplies energy to a body. There are 20 different naturally occurring amino acids that make all types of protein. Proteins come in various sizes and shapes. Some comes in a thread-like shape known as fibrous proteins and they tend to have structural or mechanical roles. Others come in spherical shapes, known as the globular proteins [16]. These spherical proteins function as enzymes, transport proteins, or antibodies. The key function of protein is based on its ability to recognize and bind specific ally to molecules, it also need to be in the right shape in other to function properly [15]. The primary structure of proteins is a linear sequence of amino acids encoded by DNA. This sequence controls how protein folds into three dimensional structure, the stability of its resulting structure [17], and functions. It is important to add that protein is an important building block of bones, skin, blood and

When a subunit binds to oxygen, it changes it conformation and sends messages to other subunits to bind to oxygen as well. When more hemoglobin monomers (subunits) bind to oxygen, it is increasing hemoglobin’s affinity to oxygen, thus leading to better cooperativity. It was also discovered that there is a higher affinity for purified hemoglobin rather than the hemoglobin inside the red blood cells due to the anionic compound 2,3-bisphosphoglycerate (2,3-BPG). This molecule binds to hemoglobin in a small pocket only found in the T state when it is deoxygenized and allows it become stable. It further causes a reduction in hemoglobin’s affinity to oxygen, working out in its favor. During the transition from T to R state, the pocket containing 2,3-BPG is broken and

For the second part of the experiment, one had to use the knowledge learn from viewing protein molecules in FirstGlance in Jmol to analyze the protein PDB ID: 4EEY. The analysis of this protein was done using the RSCB protein data bank (PDB) at (http://www.rcsb.org/pdb/home/home.do).2

Thrombin is a naturally occurring protein that is present in the blood of humans and animals. The main function of thrombin is as an intermediate step during hemostasis, which slows bleeding by forming blood clots. Thrombin acts as an enzyme during an injury, converting fibrinogen to fibrin, which then causes blood clots to form. Due to its properties, thrombin’s application to the medical field includes topical surgery in the case of minor injuries as well as various other medical procedures such as neurosurgical operations. Apart from applications in the medical field, thrombin also plays significant roles by directly interacting with endothelial cells throughout the body.

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

Blood chemistry or blood test is identifying the different levels of chemical ingredients found in the blood. The analysis of these substances provides clues to a patient’s condition and the functioning of the major body systems such as, blood sugar levels, liver functions, essential nutrients etc. This helps doctors in diagnosing the patient’s conditions much easier and quicker.