Diary of (Sort of) a Chemical Biologist

The original article is here :   Regulated N-glycosylation controls chaperone function and receptor trafficking | Science One of my past research projects involved oligosaccharyltransferase (OST). Personally, I do not like working with transmembrane enzymes, like OST, but  one thing that's always intrigued me about OST or other post-translational modification synthetic enzymes (e.g. O-GlcNAc transferase), is their promiscuity—how do these enzymes work on such a wide variety of substrates? I mean, this paper is not about enzymology of OST, but the central question the paper ask in the introduction section is  compelling: Can the activity of OST be modulated by other factors?  Researchers figured out the N-terminal region of HSP90B1 (ER chaperone) plays a regulatory role in modulating OST activity. Essentially, they propose that this region can act as a pseudo-substrate , inhibiting the glycosylation activity of OST. Very cool!  How did evolution shape H...

Original article is here (  Five protein-design questions that still challenge AI ) This article brings an insightful snapshot for anyone interested in protein design, expecially non-expert (such as me!) consideing starting their own mini-project in this field. As an enzymologist, one of the striking aspects of the article is the emphasis on protein conformation . We often overlook the fact that proteins and enzymes are not static - they are indeed dynamic molecules. The structures we see are merely snapshots of one moment in time, but they does not necessarily capture the full extent of the protein's motion.  If protein dynamics are a 4-dimensional problem, perhaps designers are only starting to scratch the surface, seeking to understand this complexity in a simplified form. (I mean how many enzyme people run MD by themselves?) This raises a question: can we truly extract or capture protein dynamics just from sequence information alone? This seems like a huge challenge, expec...

 (Writing)