Prion Essay

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Out of the many forms of infectious agents, one that seemingly defies the central dogma of biology is the prion. These types of diseases are created when an otherwise suitable protein is altered in a prion like domain, becomes misfolded, and begins contorting other specimens of the same protein to this misfolded shape resulting in what’s known as an amyloid fiber. This entire replication process does not require DNA, simply more of the non-mutated protein. Recent studies focusing on mutations identified in two heterogeneous nuclear ribonucleicprotiens, hnRNPA2B1 and hnRNPA1, have shown to produce cytoplasmic inclusions. This causes mass degradation of muscle tissues and structures throughout the human body known as multisystem …show more content…

Results of exploration Creation and Spreading of Prions
A prion disease is defined when an altered form of a protein is capable of catalyzing a near identical change in another copy of the stated protein.These can be transmitted via an altercation of the protein as it is generated, or through the interactions of normal proteins with the mutated variety. Many yeast, fungal, and human prion diseases form amyloids. These fibers are characterized by a β-sheet rich conformation. Generally these sheets are highly repetitive, and therefore have a high propensity to self-assemble and perpetuate throughout the cell. Generally these areas of high repetition, or prion forming domains (PFDs), are intrinsically disordered and are rich in glutamine and asparagine. According to a study done by Ricardo Sant’Anna et al. four yeast proteins contain protein domains fitting this characterization; Mot3, Sup35, Swi1, and Ure2; have a high likelihood of aggregating into β-sheet rich amyloid fibrils. Using infrared spectroscopy this experiment was able to show that these proteins convert from the normal disordered coil structure into one that has a rich B-sheet configuration when placed under stress. Upon further investigation these amyloid structures were displaying a cross-B structure that could build into a larger amyloid fiber. This experiment

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