Sandbox Reserved 198: Difference between revisions
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The synthesis of proteins allowed scientists to analyze biological molecules through manipulations that could not readily be made with natural proteins. These syntheses, though, were very difficult, required large investments of time, and advances in technique did not occur frequently. At the beginning of the twentieth century, Emil Fischer performed the first synthesis of a peptide, but it was not until 1953 that the first peptide hormone was synthesized by Du Vigneaud. The development of solid phase synthesis by Bruce Merrifield was a radical departure from traditional methods of bio-molecular synthesis that greatly increased efficiency. His method made possible the syntheses of much larger and more complex molecules; however, solid phase synthesis was not fully embraced until he demonstrated its full ability with the complete synthetic synthesis of Ribonuclease A. This milestone synthesis and subsequent semisynthetic syntheses of enzymes including RNase A enriched the hypothesis that the amino acid sequence of a protein contains all necessary information to direct the formation of a fully active enzyme and, additionally, that an enzyme demonstrating the catalytic capacity and specificity of a naturally produced enzyme can be made in laboratory. | The synthesis of proteins allowed scientists to analyze biological molecules through manipulations that could not readily be made with natural proteins. These syntheses, though, were very difficult, required large investments of time, and advances in technique did not occur frequently. At the beginning of the twentieth century, Emil Fischer performed the first synthesis of a peptide, but it was not until 1953 that the first peptide hormone was synthesized by Du Vigneaud. The development of solid phase synthesis by Bruce Merrifield was a radical departure from traditional methods of bio-molecular synthesis that greatly increased efficiency. His method made possible the syntheses of much larger and more complex molecules; however, solid phase synthesis was not fully embraced until he demonstrated its full ability with the complete synthetic synthesis of Ribonuclease A. This milestone synthesis and subsequent semisynthetic syntheses of enzymes including RNase A enriched the hypothesis that the amino acid sequence of a protein contains all necessary information to direct the formation of a fully active enzyme and, additionally, that an enzyme demonstrating the catalytic capacity and specificity of a naturally produced enzyme can be made in laboratory. | ||
[[Image:13027382714469.png|300 px |]] | |||
Two-dimesional representation of Semisynthetic RNase A. The synthetic peptide analog, RNase 111-118, is colored according to hydrophilicity. Yellow areas are comprised of hydrophobic residues. Red and brown segments are negatively and positively charged residues, respectively. | |||
<scene name='Sandbox_Reserved_198/Semisynthetic_rnase_a/1'>Semisynthetic RNasa A</scene> | <scene name='Sandbox_Reserved_198/Semisynthetic_rnase_a/1'>Semisynthetic RNasa A</scene> | ||
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