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Project

For those who are sceintifically inclined and like interesting problems people tackle, I am gonna try my head at this…

N-Linked Glycosylation

Because it has very deep rooted and fundamental effects on a thousand things including, very very importantly to biology, this….

If you wanna know more, drop me a line.

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This was written by Nash. Posted on Monday, April 18, 2005, at 00:34. Filed under All. Bookmark the permalink. Follow comments here with the RSS feed. Post a comment or leave a trackback.
  • AshD

    Why! Why! Why’ve you posted that pathway here! I was glad to get over with it in Ist Sem…and now I see it again! Btw you need any help on that? U’ve already visited my blog http://intoashd.blogspot.com/

    I’m doing my Masters in Molecular Biology.

  • AshD

    Why! Why! Why've you posted that pathway here! I was glad to get over with it in Ist Sem…and now I see it again! Btw you need any help on that? U've already visited my blog <a href="http://intoashd.blogspot.com/<br&quot; target="_blank"><a href="http://intoashd.blogspot.com/<br</a>&quot; target="_blank">http://intoashd.blogspot.com/<br</a></a&gt; /><br />I'm doing my Masters in Molecular Biology.

  • Nash

    I posted, with some intention of writing more detail about it. Which of course I never got around to.
    As for any help : here is what the project is…

    We have crystallographic (~2 angstrom resolution) structures of several glycosylated proteins and we want to look at a topological or free energy consensus for site and type of N-glycosylation. A sequon has been known for several years , Asn-X-Ser/Thr. However, the sequon is only a pre-requisite and not indication of a glycosylation site.
    Some of the proteins we have expressed in E.coli and found aberrant glycosylation. In vitro glycosylation also gave the same results…aberrant. We think that the high specificity comes from topological features of the folded/misfolded proteins.

    Glycosylation improves therapeutic value of almost all peptide pharmaceuticals. However, the industry achieves at best aberrant glycosylation like I mentioned before. The FDA does not permit a product to go onto the market whose exact nature is not known. Hence the interest in figuring out where the specificity in the process lies.

    If you got ideas, I am always open to them.

  • Nash

    I posted, with some intention of writing more detail about it. Which of course I never got around to.<br />As for any help : here is what the project is…<br /><br />We have crystallographic (~2 angstrom resolution) structures of several glycosylated proteins and we want to look at a topological or free energy consensus for site and type of N-glycosylation. A sequon has been known for several years , Asn-X-Ser/Thr. However, the sequon is only a pre-requisite and not indication of a glycosylation site.<br />Some of the proteins we have expressed in E.coli and found aberrant glycosylation. In vitro glycosylation also gave the same results…aberrant. We think that the high specificity comes from topological features of the folded/misfolded proteins. <br /><br />Glycosylation improves therapeutic value of almost all peptide pharmaceuticals. However, the industry achieves at best aberrant glycosylation like I mentioned before. The FDA does not permit a product to go onto the market whose exact nature is not known. Hence the interest in figuring out where the specificity in the process lies.<br /><br />If you got ideas, I am always open to them.