Sandbox Reserved 198: Difference between revisions

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>. The crystal structure similarities of the <scene name='Sandbox_Reserved_198/Wild_type_as/1'>Wild Type Active Site</scene> and the Fully Synthetic Active Site are further evidence that amino acid sequence dictates folded structure formation.