Sandbox Reserved 198: Difference between revisions

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~~<scene name='Sandbox_Reserved_198/Interface/8'>Interface - Zoom</scene>~~

<Structure load='1SRN' size='450' frame='true' align='left' caption='~~Fully Synthetic RNasa A~~

Residues 114-124 are highlighted in the surface representations of the Wild Type, Fully Synthetic, and Semisynthetic enzymes to emphasize similarity in structure. Also, the surface representation of semisynthetic RNase A illustrates the interface between the synthetic analog and the natural enzyme ' scene='Sandbox_Reserved_198/Fully_synthetic/4' />

=='''Structure equals Function'''==

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''Semisynthetic RNase A''

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>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the C terminal residues <scene name='Sandbox_Reserved_198/Synthetic_component/3'>111-124</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the <scene name='Sandbox_Reserved_198/Interface/7'>semisynthetic enzyme</scene> adopts a structure that closely resembles that of <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type RNase A</scene><ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. The restoration of the structure reconstitutes the enzymatic activity of RNase to 98%<ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>.

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>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the C terminal residues <scene name='Sandbox_Reserved_198/Synthetic_component/3'>111-124</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the <scene name='Sandbox_Reserved_198/Interface/7'>semisynthetic enzyme</scene> <scene name='Sandbox_Reserved_198/Interface/8'>(Zoom)</scene> adopts a structure that closely resembles that of <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type RNase A</scene><ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. The restoration of the structure reconstitutes the enzymatic activity of RNase to 98%<ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>.

''Fully Synthetic RNase A''

Sandbox Reserved 198: Difference between revisions

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+<Structure load='1SRN' size='450' frame='true' align='left' caption='Residues 114-124 are highlighted in the surface representations of the Wild Type, Fully Synthetic, and Semisynthetic enzymes to emphasize similarity in structure. Also, the surface representation of semisynthetic RNase A illustrates the interface between the synthetic analog and the natural enzyme  ' scene='Sandbox_Reserved_198/Fully_synthetic/4' />
-<scene name='Sandbox_Reserved_198/Interface/8'>Interface - Zoom</scene>
-<Structure load='1SRN' size='450' frame='true' align='left' caption='Fully Synthetic RNasa A
-Residues 114-124 are highlighted in the surface representations of the Wild Type, Fully Synthetic, and Semisynthetic enzymes to emphasize similarity in structure. Also, the surface representation of semisynthetic RNase A illustrates the interface between the synthetic analog and the natural enzyme  ' scene='Sandbox_Reserved_198/Fully_synthetic/4' />
 =='''Structure equals Function'''==
@@ Line 30: / Line 25: @@
 ''Semisynthetic RNase A''
-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>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the C terminal residues <scene name='Sandbox_Reserved_198/Synthetic_component/3'>111-124</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the <scene name='Sandbox_Reserved_198/Interface/7'>semisynthetic enzyme</scene> adopts a structure that closely resembles that of <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type RNase A</scene><ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. The restoration of the structure reconstitutes the enzymatic activity of RNase to 98%<ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>.
+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>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. However, a complex of RNase 1-118 with a synthetic polypeptide comprising the C terminal residues <scene name='Sandbox_Reserved_198/Synthetic_component/3'>111-124</scene> restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the <scene name='Sandbox_Reserved_198/Interface/7'>semisynthetic enzyme</scene> <scene name='Sandbox_Reserved_198/Interface/8'>(Zoom)</scene> adopts a structure that closely resembles that of <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type RNase A</scene><ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>. The restoration of the structure reconstitutes the enzymatic activity of RNase to 98%<ref>Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry 262.33 (1987): 15930-5938.</ref>.
 ''Fully Synthetic RNase A''