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]. 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.

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 <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. 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''' ==

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].  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.
+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 <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. 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''' ==