Sandbox Reserved 197: Difference between revisions

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== '''Introduction''' ==

Ribonuclease A is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. ~~There are several features of its structure that are pertinent to its folding and function and~~ RNase A ~~has been used time~~ and ~~again to illustrate these important features of protein folding~~. The active site ~~of a protein is where the actually binding of the protein to its substrate(s) occur(s) and the~~ <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> ~~of Rnase A~~ lies within ~~its~~ cleft. ~~Proteins form~~ interactions ~~between different parts~~ of ~~their~~ structure ~~for stabilization~~. ~~In RNase A, there are~~ eight cysteine residues ~~present~~ that form four disulfide ~~linkages that contribute to the ordered structure as well as the speed of folding of RNase A. Another important aspect to folding of its is the presence of two~~ ''cis'' proline residues.

Ribonuclease A is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through [[crystallography]] [http://en.wikipedia.org/wiki/Crystallography] and [[FABMS]] [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. RNase A is composed of four anti-parallel B-sheets and 3 a-helixes. The active site <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Interatomic interactions are important for stabilization and the folding mechanism of the structure. Presence of eight cysteine residues that form four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A.

== '''Folding''' ==

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.

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 site directed mutagenesis to wildtype RNase A. 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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@@ Line 7: / Line 7: @@
 == '''Introduction''' ==
-Ribonuclease A is an enzyme involved in catalyzing RNA degradation.  The structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  There are several features of its structure that are pertinent to its folding and function and RNase A has been used time and again to illustrate these important features of protein folding.  The active site of a protein is where the actually binding of the protein to its substrate(s) occur(s) and the <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> of Rnase A lies within its cleft.  Proteins form interactions between different parts of their structure for stabilization.  In RNase A, there are eight cysteine residues present that form four disulfide linkages that contribute to the ordered structure as well as the speed of folding of RNase A.  Another important aspect to folding of its is the presence of two ''cis'' proline residues.
+Ribonuclease A is an enzyme involved in catalyzing RNA degradation.  The structure of RNase A has been determined through [[crystallography]] [http://en.wikipedia.org/wiki/Crystallography] and [[FABMS]] [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  RNase A is composed of four anti-parallel B-sheets and 3 a-helixes. The active site <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Interatomic interactions are important for stabilization and the folding mechanism of the structure. Presence of eight cysteine residues that form four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A.
 == '''Folding''' ==
-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.
+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 site directed mutagenesis to wildtype RNase A.  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'''===