Sandbox Reserved 197

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== '''Introduction''' ==
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Ribonuclease A is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through crystallization and FABMS. There are several features of its structure that are pertinent to its folding and function. The catalytic residues of RNase A include His12, His 119, and Lys41. The active site lies within its cleft. RNase A has eight cysteine residues present that form four disulfide linkages which contribute to the ordered structure that has been observed as well as the speed of folding. Another important aspect to folding is the presence of two ''cis'' proline residues.

Revision as of 15:15, 28 March 2011

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This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200.
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Introduction

Ribonuclease A is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through crystallization and FABMS. There are several features of its structure that are pertinent to its folding and function. The catalytic residues of RNase A include His12, His 119, and Lys41. The active site lies within its cleft. RNase A has eight cysteine residues present that form four disulfide linkages which contribute to the ordered structure that has been observed as well as the speed of folding. Another important aspect to folding is the presence of two cis proline residues.

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