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| - Semisynthesis of a Glycosylated Im7 Analogue for ProteinFolding Studies
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| - To establish a system to address questions concerning the influence of glycosylation on proteinfolding pathways, we have developed a semisynthetic route toward the immunity protein Im7. This fourhelix protein has been used extensively as model protein for folding studies. Native chemical ligation (NCL)affords an N-linked chitobiose glycoprotein analogue of Im7 with an Ala29Cys mutation. The semisyntheticapproach relies on the solid-phase peptide synthesis (SPPS) of N-terminal thioesters (including helix I), inglycosylated or unglycosylated form, in combination with the expression of the C-terminal fragment of Im7(containing helices II−IV). Detailed kinetic and thermodynamic analysis of the protein folding behavior revealsthat semisynthetic Im7 analogues are well suited for protein folding studies and that the folding mechanismof the glycoprotein of this Im7 variant is not significantly altered over the unglycosylated analogue.
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