Creutzfield Jakob Disease
Who would of thought that eating hamburgers, steaks and drinking milk could produce an epidemic disease? These types of food are frequently eaten for their appealing tastes and nutritional values. The discovery of Creutzfeld Jakob Disease (CJD) has been a long and remarkable one. The cause of this disease is a mutated prion protein within the brain that can be either inherited or acquired. These mutations create sponge like holes that destroy the brain. As a result, the disorder gives both behavioural and muscular problems to infected individuals Experiments and discoveries to this disease have led to a further understanding of the diversity of proteins. In the 1960s, D. Carleton Gadjusek studied the behaviour of a native population in Papua, New Guinea. This population had been eating the brains of dead relatives and as a result, contracted a fatal neurodegenerative disease. When autopsies were taken from the population who died, they appeared to have a distinct pathology. The central brain tissue resembled a sponge with a lot of regions containing microscopic holes. The results of this disease appeared similar to persons affected with CJD. In 1968, D. Carleton Gadjusek injected an infected biopsy of brain with this disorder into
a laboratory animal. As a result, the animal developed this disease. At this time, the biopsy was thought to contain a virus. At the University of California, Stanley Pruisner and colleagues proposed that agent for this disease was a prion. A prion is a protein version of viruses without the genetic information. Once the prion has entered the body, the normal proteins are mutated. The gene for the normal protein is expressed within normal brain tissue and encodes a protein that resides at the surface of nerve cells. The function is unknown. The mutated prion version of the protein accumulates within nerve cells, forming aggregates that kill cells. The normal protein is soluble in salt solution and is destroyed by protein-eating molecules, known as enzymes. However, the mutated prion protein is insoluble and the protein digestion. Based on these differences, one might expect these two forms of the prion protein to be composed distinctly different sequences of amino acids, but this is not the case. Prions are proteins, a diverse group of macromolecules. Proteins are capable of a wide variety of functions and activities. This is due to the great variety of structures. Proteins are polymers of amino acids known as polypeptides. These amino acids are the structural building blocks of proteins. Amino acids have a single carbon linked to: an amino group, a carboxylic acid group and a side chain. These side chains vary in structure and determine the chemical properties of the amino acids. Each protein has a unique and highly ordered structure that is highly specific with the molecules it interacts with. The assortment of the twenty amino acids are important because of the activities the protein can perform in terms of both the intramolecular interactions and intermolecular interactions. Intramolecular interactions are the forces within a molecule. It could be thought of as intramural collegiate activities, interactions within a molecule. Inte
Some topics in this essay:
Stanley Pruisner,
Lymphotoxin LT,
Encephalopathy BSE,
Papua Guinea,
Disease CJD,
England Switzerland,
Carleton Gadjusek,
,
mutated prion,
prion protein,
amino acids,
mutated prion protein,
normal mutated,
secondary structure,
intermolecular interactions,
normal prions,
immune cells,
normal protein,
mad cow disease,
cow disease,
normal mutated proteins,
proteins primary structure,
bonds elements peptide,
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Approximate Word count = 1313
Approximate Pages = 5 (250 words per page double spaced)
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