Sandbox Reserved 197: Difference between revisions

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==''Medical Importance''==

Protein folding, along with its inhibitions, is immensely important to the human. Such diseases as ALS, Alzheimer's Disease, and Parkinson's Disease can all be traced back to the protein. Proteins can form aberrant aggregates when they do not fold correctly. This abnormaility can be fatally toxic to the human nerve cells. During folding, proteins sometimes make a mistake. Each protein contains <scene name='Sandbox_Reserved_197/Hydrophobic-hydrophilic/1'>hydrophobic and hydrophilic residues</scene>. In the case of these aggregates, the mistake exposes "sticky" <scene name='Sandbox_Reserved_197/Hydrophobic/1'>hydrophobic patches</scene> that can cause several proteins to stick to one another. In the future researchers hope to design drugs that combat this mistake in the protein folding. The use of ribonuclease A in protein folding research has been an instrumental feature in designing experiments to determine these "misfolding" snapshots and in developing therapies to prevent this problem in the future.

Protein folding, along with its inhibitions, is immensely important to the human. Such diseases as ALS, Alzheimer's Disease, and Parkinson's Disease can all be traced back to the protein. Proteins can form aberrant aggregates when they do not fold correctly. This abnormaility can be fatally toxic to the human nerve cells. During folding, proteins sometimes make a mistake. Each protein contains <scene name='Sandbox_Reserved_197/Hydrophobic-hydrophilic/1'>hydrophobic and hydrophilic residues</scene>. The hydrophilic residues lie on the outer part of the protein and the hydrophobic residues bury themselves due to the [[hydrophobic effect]]. In the case of these aggregates, the mistake exposes "sticky" <scene name='Sandbox_Reserved_197/Hydrophobic/1'>hydrophobic patches</scene> of the interior that can cause several proteins to stick to one another. In the future researchers hope to design drugs that combat this mistake in the protein folding. The use of ribonuclease A in protein folding research has been an instrumental feature in designing experiments to determine these "misfolding" snapshots and in developing therapies to prevent this problem in the future.

=='''References'''==

Sandbox Reserved 197: Difference between revisions

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 ==''Medical Importance''==
-Protein folding, along with its inhibitions, is immensely important to the human.  Such diseases as ALS, Alzheimer's Disease, and Parkinson's Disease can all be traced back to the protein.  Proteins can form aberrant aggregates when they do not fold correctly.  This abnormaility can be fatally toxic to the human nerve cells.  During folding, proteins sometimes make a mistake.  Each protein contains <scene name='Sandbox_Reserved_197/Hydrophobic-hydrophilic/1'>hydrophobic and hydrophilic residues</scene>. In the case of these aggregates, the mistake exposes "sticky" <scene name='Sandbox_Reserved_197/Hydrophobic/1'>hydrophobic patches</scene> that can cause several proteins to stick to one another.  In the future researchers hope to design drugs that combat this mistake in the protein folding.  The use of ribonuclease A in protein folding research has been an instrumental feature in designing experiments to determine these "misfolding" snapshots and in developing therapies to prevent this problem in the future.
+Protein folding, along with its inhibitions, is immensely important to the human.  Such diseases as ALS, Alzheimer's Disease, and Parkinson's Disease can all be traced back to the protein.  Proteins can form aberrant aggregates when they do not fold correctly.  This abnormaility can be fatally toxic to the human nerve cells.  During folding, proteins sometimes make a mistake.  Each protein contains <scene name='Sandbox_Reserved_197/Hydrophobic-hydrophilic/1'>hydrophobic and hydrophilic residues</scene>.  The hydrophilic residues lie on the outer part of the protein and the hydrophobic residues bury themselves due to the [[hydrophobic effect]]. In the case of these aggregates, the mistake exposes "sticky" <scene name='Sandbox_Reserved_197/Hydrophobic/1'>hydrophobic patches</scene> of the interior that can cause several proteins to stick to one another.  In the future researchers hope to design drugs that combat this mistake in the protein folding.  The use of ribonuclease A in protein folding research has been an instrumental feature in designing experiments to determine these "misfolding" snapshots and in developing therapies to prevent this problem in the future.
 =='''References'''==