1. An interesting to look at the role of glycosylation in influenza infection by exploring the mechanism of action of one of the only effective therapies against the virus - Tamiflu. To begin discussion ask a simple question: From a protein structure/function standpoint, what role does glycosylation play during influenza infection? What does the future have in store for NA inhibitors?
2. Reversible protein phosphorylation is a critical mediator of cellular physiology that many of you are already familiar with from your previous coursework or from last week's assignment.
What is the role of phosphorylation with respect to the Tau protein?
How does the presence of multiple phosphorylation sites complicate our understanding it's regulation (or does it?).
Keeping with our ongoing theme of protein evolution - is this a selective advantage, side effect, or something else entirely?
3. Nearly 50% of all drugs currently under modulate protein phosphorylation and the vast majority of them will fail.
Why? What is attractive about ubiquitin ligases in comparison to kinases/phosphatases with respect to drug development?