Hemoglobin Research Paper

Sickle Cell Anemia is a disease that affects how oxygen is carried throughout the body by blood. Specifically, sickle cell anemia is characterized by a change in the shape of red blood cells from a smooth donut shape to a crescent or sickled shape. The sickled cells are very long and stiff, so many times

Sickle Cell anemia is a group of inherited red blood cell disorders, or a collection of recessive genetic disorders characterized by a hemoglobin variant called Hb S. Normal red blood cells are round like doughnuts, and they move through small blood tubes in the body to deliver oxygen. Sickle red blood cells become hard, sticky and shaped like sickles used to cut wheat. When these hard and pointed red cells go through the small blood tube, they clog the flow and break apart. This can cause pain, damage and a low blood count, or anemia. There is a substance in the red cell called hemoglobin that carries oxygen inside the cell. One little change in this substance causes the hemoglobin to form long hard rods in the red cell when it gives

The disease is caused by a mutated version of the gene that help makes hemoglobin. Hemoglobin is the protein that carries oxygen in red blood cells. Sickle cell is a disorder in the blood caused by abnormal hemoglobin proteins. The abnormal hemoglobin protein caused sickle cell shaped red blood cells. The sickle cell red blood cells are crescent shapes and can clog up very easily in blood canals. In the diagram to the right it shows how a mutation causes a change in the amino acid.

Transport proteins such as Haemoglobin carry oxygen through the blood. Myoglobin performs a similar function in muscle tissue, taking oxygen from the haemoglobin in the blood and storing it or carrying it around until needed by the muscle cells. The ability of haemoglobin to bind oxygen is sensitive to several factors. They include pH, temperature, concentrations of O2 and CO2. The structure of the haemoglobin changes slightly in a way that makes it better at binding to more oxygen, further enhancing its ability to carry more oxygen. Sickle cell anaemia points out another important aspect of protein structure. The mutation of a base sequence leads to valine being produced instead of glutamic acid, this has a knock on effect on the secondy, tertiary and quaternary structure. All in all the function of Hb is altered and results in the Hb having a “sickled shape” which does not easily pass though capillaries or carry oxygen efficiently. Cytochromes operate in the electron transport chain as electron carrier proteins (fact from Google)

People suffering from sickle cell disease has haemoglobin S replacing at least one of the beta-globin tertiary subunits in haemoglobin. In the case of sickle cell anaemia, both beta-globin subunits are replaced by haemoglobin S. There are other types of sickle cell disease in which one beta- globin is replaced by haemoglobin S and the other replaced by haemoglobin C which is another type of mutation variant of the beta-globin subunit of haemoglobin.

All of the cells within the tissues of the body need a regular supply of oxygen to function. The hemoglobin found in red blood cells (RBC’s) are essential for the proper transport of oxygen molecules. They bind oxygen in the lungs and carry to every tissue within the body. Due to the structure of hemoglobin, normal RBC’s are donut shaped with a concaved center. This flexible shape is what allows the BRC’s to move freely into very small spaces such as capillaries where they will deliver their oxygen. Sickle cell anemia or other diseases that fall within the broader group of disorders characterized by SCD describe conditions where the protein (hemoglobin) has misfolded and altered the shape of the cell. Sickle hemoglobin allows for the formation of stiff rods within the red blood cell giving it a sickle, or crescent shape. This new shape is not flexible and can block or slow the flow of blood. When this occurs, oxygen cannot reach its intended tissues. This results in severe pain called crises, and these attacks occur

But when abnormal sickle haemoglobin releases the oxygen, the oxygen sticks together and forms long rods, which damage and change the red blood cell into rigid, sticky, sickle like or crescent moon shapes.

Sickle-cell Anemia is a disorder that is typically inherited from a person's parents. Sickle-cell anemia results in an abnormality in the oxygen-carrying protein haemoglobin (haemoglobin S) that is found in red blood cells. In such a condition the red blood cells contort into a sickle shape. The affected cells die early which results to a shortage of healthy red blood cells and can block blood flow causing pain. The disease s caused by gene mutation through the process of substitution. In the Sickle-cell condition one Amino Acid; glutamic acid is always replaced by another acid valine. This happens in each of the two polypeptide chains of the haemoglobin molecule.This alteration results to a haemoglobin type S that is defective and is genetically

Sickle Cell Trait hereditary pattern is autosomal recessive. Meaning two copies of Sickle Cell Trait must be present for the disease to be expressed. People who inherited a single copy of Sickle Cell Trait express no disease and live normal lives. Both copies of Sickle Cell Trait cause a SNP mutation in the Hemoglobin Beta Gene, located on chromosome 11q15. A single thymine molecule gets replaced by a adenine molecule. This single molecule mutation causes the person to produce mutated Beta-Globin. Beta-Globin is an essential piece of of the protein Hemoglobin, a single Hemoglobin protein is comprised of two Beta-Globins and two Alpha

Sickle cell anemia (SCA) is one of the most common severe monogenetic disorders in the world. (1).SCA is an inherited blood disorder caused by a single point mutation in one of the genes encoding hemoglobin (2).Hemoglobin (Hb) it is an oxygen transporting molecule, carrying oxygen from the lungs to the tissues and takinge carbon dioxide away from the cell. Hb, made of four globin protein chains two alpha and two beata chains (pic).http://themedicalbiochemistrypage.org/images/hemoglobin.jpg

A genetic disorder caused by the abnormal gene for hemoglobin S is called sickle cell anemia. Only replace that take place in glutamic acid is to fill in for valine as the sixth codon of the hemoglobin protein, which alter declines the hemoglobin’s ability transform oxygen throughout your body. The human body needs oxygen in order to function when we eat food and liquid for energy even including muscles, repairs our cells, feeds our brain, breath and nerves. Normal cells are described as round, red, flexible and travel easily throughout your blood vessels. Sickle cell anemia describes a red blood cell that has inflexible, tacky, and create like a crescent moons not like the normal red cells. It tends to slow down or block the blood flows while

Sickle-cell disease majorly affects the hemoglobin that is present in our blood. The job of hemoglobin is to help transport oxygen and carbon dioxide to and from the cells throughout our body. Hemoglobin is present specifically in our red blood cells. Each red blood cell contains two hundred and eighty million hemoglobin molecules. Red blood cells normal shape is a biconcave shape because of the lack of many organelles and a nucleus. The shape is so important to a red blood cells functioning that if it is not shaped normally it has major consequences. The shape helps them to fit through capillaries easier and also allows for an increased surface area which results in easier gas exchange. Sickle-cell disease is a genetic disease that causes issues in the oxygen/carbon dioxide carrying hemoglobin molecules that are present in our red blood cells.

Sickle cell disease is a group of diseases in which the affected individual has at least one copy of hemoglobin S (HbS). Sickle cell anemia is a type of sickle cell disease in which the patient inherits 2 copies of hemoglobin S (genotype HbSS). There are other examples of sickle cell disease; they include- HbAS, HbSC, and HbS beta thalassemia (National Heart, Lung, and Blood Institute). The focus of this article would be on Sickle cell anemia. Sickle cell anemia is seen predominantly among Africans but is also seen in people of Mediterranean origin and the Middle East. It occurs in approximately 1:500 African American births and 1:36,000 Hispanic American births. About 2 million people in the United States have acquired the sickle cell trait (U.S. Department of Health and Human Services). The disease is caused by a point mutation in position 6 of the beta subunit of the hemoglobin gene which results in substitution of the amino acid valine in place of glutamic acid. There is a single nucleotide substitution (A to T) in the codon for amino acid 6. The change converts a glutamic acid codon (GAG) to a valine codon (GTG) (National Heart, Lung, and Blood Institute).

Sickle Cell Anemia is a disease that affects how oxygen is carried throughout the body by blood. Specifically, sickle cell anemia is characterized by a change in the shape of red blood cells from a smooth donut shape to a crescent or sickled shape, almost the same shape as a crescent moon. The sickled cells are very long and stiff, so sometimes

Myoglobin consist of single polypeptide chain that made up of 153 amino acid and ahs a size of 18 kDa. Its three-dimensional structure was first determined by X-ray crystallography by John Kendrew in 1957. Myoglobin is a typical globular protein in that it is a highly folded compact structure with most of the hydrophobic amino acid residues buried in the interior and many of the polar residues on the surface. X-ray crystallography revealed that the single polypeptide chain of myoglobin consist of entirely of eight (labelled A-H) alpha-helical. Within a hydrophobic crevice formed by the folding polypeptide chain is the heme prosthetic group. This nonopolypepetide unit is noncovalently bound to myoglobin and is essential for the biological