Sandbox Reserved 197: Difference between revisions

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== '''Folding''' ==

There are features of every protein that directly or indirectly effect the folding of that protein. Several of these features have been identified in RNase A by the use of mutants of the native form. These mutations and the study of the kinetics and final structure in comparison to the native form show whether that particular feature is involved in the folding of the protein.

There are features of every protein that directly or indirectly effect the folding of that protein [http://en.wikipedia.org/wiki/Protein_folding]. Several of these features have been identified in RNase A by the use of mutants of the native form. These mutations and the study of the kinetics and final structure in comparison to the native form show whether that particular feature is involved in the folding of the protein.

==='''Proline Conformation'''===

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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>. The hydrophilic residues lie on the outer part of the protein and the hydrophobic residues bury themselves due to the [http://en.wikipedia.org/wiki/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.

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 [http://en.wikipedia.org/wiki/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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@@ Line 10: / Line 10: @@
 == '''Folding''' ==
-There are features of every protein that directly or indirectly effect the folding of that protein.  Several of these features have been identified in RNase A by the use of mutants of the native form.  These mutations and the study of the kinetics and final structure in comparison to the native form show whether that particular feature is involved in the folding of the protein.
+There are features of every protein that directly or indirectly effect the folding of that protein [http://en.wikipedia.org/wiki/Protein_folding].  Several of these features have been identified in RNase A by the use of mutants of the native form.  These mutations and the study of the kinetics and final structure in comparison to the native form show whether that particular feature is involved in the folding of the protein.
 ==='''Proline Conformation'''===
@@ Line 24: / Line 24: @@
 ==''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>.  The hydrophilic residues lie on the outer part of the protein and the hydrophobic residues bury themselves due to the [http://en.wikipedia.org/wiki/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.
+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 [http://en.wikipedia.org/wiki/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'''==