Sandbox Reserved 198: Difference between revisions

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OCA, Michael Slack

Revision as of 05:41, 15 April 2011 view source Michael Slack (talk \| contribs) 206 edits No edit summary ← Older edit		Revision as of 05:46, 15 April 2011 view source Michael Slack (talk \| contribs) 206 edits No edit summary Newer edit →
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	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.

	<scene name='Sandbox_Reserved_198/Fully_synthetic/4'>Fully Synthetic RNase A</scene> (124 residues) is prepared by two consecutive sets of one-pot ligations and related chemical transformations of six peptide segments (residues 1-25, 26-39, 40-64, 65-83, 84-94, 95-124) (Boerema, 2007). The six unprotected peptide segments were synthesized by highly optimized, stepwise solid-phase synthesis. This synthetic pathway is simple, has high overall yields, and it eliminate the need for the isolation of intermediate products.		The <scene name='Sandbox_Reserved_198/Fully_synthetic/4'>Fully Synthetic RNase A</scene> (124 residues) is prepared by two consecutive sets of one-pot ligations and related chemical transformations of six peptide segments (residues 1-25, 26-39, 40-64, 65-83, 84-94, 95-124) (Boerema, 2007),which can prevent undesired byproduct formation. The six unprotected peptide segments were synthesized by highly optimized, stepwise solid-phase synthesis. This synthetic pathway is simple, has high overall yields, and it eliminate the need for the isolation of intermediate products.