Sandbox Reserved 198: Difference between revisions
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=='''Synthetic Method'''== | =='''Synthetic Method'''== | ||
''Solid-Phase Peptide Synthesis'' | ''Solid-Phase Peptide Synthesis-Semisynthetic RNase A'' | ||
Peptide synthesis is the production of proteins in which multiple amino acids are linked together through peptide bonds. A general chemical requirement for peptide synthesis is the blockage of the carboxyl group of one amino acid and the amino group of the second amino acid. The carboxyl group of the free carboxyl group can be activated and the new peptide bond is formed (Merrifield, 1984). A common type of peptide synthesis is the solid-phase synthesis, in which the end of the peptide chain is attached to a solid support, as shown in Figure 1. | Peptide synthesis is the production of proteins in which multiple amino acids are linked together through peptide bonds. A general chemical requirement for peptide synthesis is the blockage of the carboxyl group of one amino acid and the amino group of the second amino acid. The carboxyl group of the free carboxyl group can be activated and the new peptide bond is formed (Merrifield, 1984). A common type of peptide synthesis is the solid-phase synthesis, in which the end of the peptide chain is attached to a solid support, as shown in Figure 1. | ||
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''Peptide Ligation'' | ''Peptide Ligation-Fully Synthetic RNase A'' | ||
The peptide ligation chemistry in addition to solid-phase peptide synthesis is used to synthesize relatively longer peptide molecules with typical length of 125 residues (Boerema, 2007). The ligation methods overcome the length limitation of solid-phase synthesis, because the chemical ligation involves the joining of mutually reactive peptide segments created by solid-phase synthesis. The peptide bond in ligation is formed between an unprotected peptide and a peptide-thioester (Boerema, 2007). The shorter peptide segments are more rapidly prepared and are less susceptible to solubility issues in longer peptide chains. | The peptide ligation chemistry in addition to solid-phase peptide synthesis is used to synthesize relatively longer peptide molecules with typical length of 125 residues (Boerema, 2007). The ligation methods overcome the length limitation of solid-phase synthesis, because the chemical ligation involves the joining of mutually reactive peptide segments created by solid-phase synthesis. The peptide bond in ligation is formed between an unprotected peptide and a peptide-thioester (Boerema, 2007). The shorter peptide segments are more rapidly prepared and are less susceptible to solubility issues in longer peptide chains. | ||
