کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1359245 | 981398 | 2010 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Multiple glycosylation of de novo designed α-helical coiled coil peptides Multiple glycosylation of de novo designed α-helical coiled coil peptides](/preview/png/1359245.png)
The aim of this study was to investigate the influence of multiple O-glycosylation in α-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six β-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil helix. Surprisingly, circular dichroism spectroscopy showed no unfolding of the coiled coil structure for all glycopeptides. Thermally induced denaturations reveal a successive but relative low destabilization of the coiled coil structure upon introduction of β-galactose residues. These first results indicate that O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies.
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Journal: Bioorganic & Medicinal Chemistry - Volume 18, Issue 11, 1 June 2010, Pages 3703–3706