Sandbox Reserved 197: Difference between revisions

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== '''Introduction''' ==
== '''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 β-sheets and 3 α-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.
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 β-sheets and three α-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 four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A.


== '''Protein Folding''' ==
== '''Protein Folding''' ==