Sandbox Reserved 198: Difference between revisions
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''Fully Synthetic RNase A'' | ''Fully Synthetic RNase A'' | ||
The <scene name='Sandbox_Reserved_198/Fully_synthetic/4'>Fully Synthetic RNase A</scene> demonstrates similar structural and functional characteristics (such as catalytic activity) as those of the <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type</scene> RNase A | The <scene name='Sandbox_Reserved_198/Fully_synthetic/4'>Fully Synthetic RNase A</scene> demonstrates similar structural and functional characteristics (such as catalytic activity) as those of the <scene name='Sandbox_Reserved_198/Wild_type/1'>Wild Type</scene> RNase A<ref>David J. Boerema, Valentina. A. T., Stephen B. H. Kent, "Total Synthesis by Modern chemical Ligation Methods and High Resolution (1.1-A) X-ray structure of Ribonuclease A. Biopolymers. 2008;90(3):278-86.</ref>. The crystal data, X-ray data collection and refinement statistics show that the fully synthetic protein shares identical molecular structures with the wild type RNase A, and that the active sites of both emzymes contain no walter molecules and have no substrate ligand<ref>David J. Boerema, Valentina. A. T., Stephen B. H. Kent, "Total Synthesis by Modern chemical Ligation Methods and High Resolution (1.1-A) X-ray structure of Ribonuclease A. Biopolymers. 2008;90(3):278-86.</ref>. | ||
=='''Synthetic Method'''== | =='''Synthetic Method'''== | ||
