Sandbox Reserved 198: Difference between revisions

Line 8:

<scene name='Sandbox_Reserved_198/Fully_synthetic/1'>Fully Synthetic</scene>

<scene name='Sandbox_Reserved_198/Synthetic_component/1'>Synthetic Component</scene>

<scene name='~~Talk:~~Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>

<scene name='Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>

<scene name='Sandbox_Reserved_198/Interface/1'>Synthetic / Natural Interface</scene>

<scene name='Sandbox_Reserved_198/Fully_synthetic/1'>Fully Synthetic</scene>

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=='''Function'''==

The structure to function relationship is clearly exhibited by semisynthetic RNase A. In the RNase A protein, the removal of six C terminal residues, leaving <scene name='~~Talk:~~Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>, completely halts enzymatic activity (Martin, 1987). However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</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 structure to function relationship is clearly exhibited by semisynthetic RNase A. 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 (Martin, 1987). However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</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).

Sandbox Reserved 198: Difference between revisions

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@@ Line 8: / Line 8: @@
 <scene name='Sandbox_Reserved_198/Fully_synthetic/1'>Fully Synthetic</scene>
 <scene name='Sandbox_Reserved_198/Synthetic_component/1'>Synthetic Component</scene>
-<scene name='Talk:Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>
+<scene name='Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>
 <scene name='Sandbox_Reserved_198/Interface/1'>Synthetic / Natural Interface</scene>
 <scene name='Sandbox_Reserved_198/Fully_synthetic/1'>Fully Synthetic</scene>
@@ Line 26: / Line 26: @@
 =='''Function'''==
-The structure to function relationship is clearly exhibited by semisynthetic RNase A. In the RNase A protein, the removal of six C terminal residues, leaving <scene name='Talk:Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>, completely halts enzymatic activity (Martin, 1987). However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</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 structure to function relationship is clearly exhibited by semisynthetic RNase A. 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 (Martin, 1987). However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</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).