Sandbox Reserved 198: Difference between revisions

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OCA, Michael Slack

Revision as of 03:53, 15 April 2011 view source Michael Slack (talk \| contribs) 206 edits No edit summary ← Older edit		Revision as of 03:55, 15 April 2011 view source Michael Slack (talk \| contribs) 206 edits No edit summary Newer edit →
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	=='''Structure equals Function'''==		=='''Structure equals Function'''==

	The synthesis of semisynthetic RNasa A clearly exhibits the structure to function relationship that defines proteins. In the RNase A protein, the removal of six C terminal residues, leaving <scene name='Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>, completely halts enzymatic activity~~<ref>~~</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Sandbox_Reserved_198/Synthetic_component/3'>C terminal residues, 111-124 Component</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the semisynthetic enzyme adopts a structure that closely resembles that of natural RNase (Martin, 1987). The restoration of the structure reconstitutes the enzymatic activity of RNase to 98% (Martin, 1987).		The synthesis of semisynthetic RNasa A clearly exhibits the structure to function relationship that defines proteins. <ref>In the RNase A protein, the removal of six C terminal residues, leaving <scene name='Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>, completely halts enzymatic activity</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Sandbox_Reserved_198/Synthetic_component/3'>C terminal residues, 111-124 Component</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the semisynthetic enzyme adopts a structure that closely resembles that of natural RNase (Martin, 1987). The restoration of the structure reconstitutes the enzymatic activity of RNase to 98% (Martin, 1987).