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Why Do Protein Misfolding

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Protein misfolding – hidden enemy of the brain
Protein has always been a fundamental and irreplaceable biomolecule that builds up life. The studying of protein, proteomics, not only allow humans be aware of ourselves and the biosphere around us but also set the foundation for scientists to approach solutions for many human’s health problems. Among those many health issues, diseases that are associated with central nervous system raise the most concern. Many of these nervous disorders, surprisingly, are caused by the misfolding of our own human’s protein rather than any infectious virus or bacteria. Indeed, protein misfolding can bring about fatal aftermaths and consequences. One of them is very well-known deadly diseases, Creutzfeld- Jakob
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As soon as the the polypeptide emerge from the ribosome, it must fold into their active native shape. A polypeptide can fold and unfold several times during its life depending on its interaction with others protein and with its surrounding environment. The polypeptide chains do not fold randomly but instead have a specific conformation. At ideal state, this conformation is manipulated by the intramolecular forces between buiding blocks of the protein molecule. To be specific, each amino acid making up of polypeptide chain or protein has different charges, polarities and functional group on its side chain. These properties, in addition with the order of the sequence of different amino acids, determine how the amino acids within the same chain will interact and how the bonds between them will be …show more content…
This disease can be both sporadic heritable and. As far as we know, the prion disease is uniquely infectious among all neurological disorders. This disease is the consequence of the misfolding of PrP protein. The folding process of protein not only depends on the properties of amino acids which the protein is made of but also on the environment condition. Therefore, as the environment in the brain is adverse or the protein itself carries mutation, the misfolding can readily occurs due to the unstable state of the protein. The result of the PrP misfolding is PrPsC proteins, which induce normal proteins to follow the misfolding pathway and aggregate to build up amyploid plague, blocking the movement of substances around and among the nerve cells. Scientists and researchers are still looking for the optimal cure for CJD by gaining thorough comprehension about protein conformation and its folding mechanism. Although this syndrome is rare compared to other neurological diseases, we still need to delve into its reaction mechanism, especially the mechanism that start the chain conversion of normal protein molecules to the misshapen prion form. Since the function of a protein is closely linked to its three-dimensional structure, prediction or experimental determination of the library of protein structures is a matter of high

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