Sandbox Reserved 197: Difference between revisions
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<Structure load='7RSA' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/1' /> | |||
== '''Introduction''' == | == '''Introduction''' == | ||
<scene name='Sandbox_Reserved_197/Rnase_a_wild_type/1'>Ribonuclease A</scene> is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through crystallography and FABMS. 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. | <scene name='Sandbox_Reserved_197/Rnase_a_wild_type/1'>Ribonuclease A</scene> is an enzyme involved in catalyzing RNA degradation. The structure of RNase A has been determined through crystallography and FABMS. 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. | ||
== '''Folding''' == | == '''Folding''' == | ||
