Day 2 At BPS – Talks, Posters, Networking, Food and Drink

Don’t worry – it’s not Groundhog Day, I had mistakenly headed my last post about Saturday at BPS as Day 2. The real Day 2 (Sunday) at the annual meeting involved – as the title suggests – Talks, Posters, Networking, Food and Drink (not in any particular order).

Let us start with the food and drinks. If you enjoy ethnic foods, a visit to the Helmand on Charles St is highly recommended.  It was actually my second visit to this Afghan restaurant, having had dinner there during my previous visit to Baltimore for BPS annual meeting ’04. They serve incredibly good food; the taste of the succulent lamb from last night is still lingering. I also recommend pairing the food with a Peter Lehman Shiraz. (do reserve, they seem to fill up quickly)

Speaking of drinks, the Pratt St Ale House is fast becoming my default ‘meeting outside the meeting’ and unwinding place. For someone from the West coast used to overly hoppy, high alcohol craft brews, the understated British style pale and brown ales here is a welcome change. Last night I found myself there with a cheerful bunch of ion channel people.  So if you see me nodding off during one of the talks today, you know who to blame!

Science-wise, there were some good talks. As expected, due to impossibility of being at two places at the same time, I must have missed out on a quite a few.

But the highlight of the day would have to be Lawrence Lee’s presentation on the structural mechanism of bacterial flagellar motion. I worked briefly at the Victor Chang Cardiac Research Institute in Sydney where Lawrence is a postdoc and had the opportunity to listen to a longer, pre-publication version of the same talk. They have very cleverly put together a convincing picture of the extremely complicated protein machinery, a structure that  is about 11MDa and comprises of 13 proteins! This molecular machine works not only at an incredible pace – greater than 100,000rpm – but can also quickly switch directions. Lee and colleagues solved the structure of one of the proteisn in this assembly, FliG, which is involved in generating the rotational torque, switching of direction and coupling of the torque to the flagellar filament. Based on the structure and mutational studies they identified putative dynamic regions and sites for polymerization (there are 34 copies of the protein in the assembly) – leading to a model of the complete assembly. As other’s have already point out, this work is much better conveyed when you look at the movies and the structural images, so do check out their recent paper in Nature.

Another New and Notable speaker, Dr Karen Fleming presented data on a new hydrophobicity scale. I did notice that the old question of the energy cost of inserting polar residues such as Arginine into the membrane is still being settled. This question goes back to the structure of the voltage-sensor domain of potassium channels and the amount of movement of that ‘paddle’, whether it twists a bit or translocates through the entire bilayer. I believe there is a little more consensus on the issue (I have not followed the field too closely recently), but I do remember the energetic debates on the nature of the paddle movement back during the ’04 annual meeting in one of the subgroup sessions.

Apart from the talks, the best of the part of the day was spent reconnecting with numerous scientific colleagues. These are people I usually see only at this meeting, especially the people from overseas. I have always found this kind of networking at Biophysics to be extremely helpful.

Speaking of networking: I would like to repeat the suggestion for having a blogger/tweeters meetup during the conference. Tonite’s society reception and dance might be a good opportunity. Do tweet if you are interested.

Before signing off for now, some geek humor from BPS members on Twitter. Do chime in.

Advertisements

Leave a Reply

Fill in your details below or click an icon to log in:

WordPress.com Logo

You are commenting using your WordPress.com account. Log Out / Change )

Twitter picture

You are commenting using your Twitter account. Log Out / Change )

Facebook photo

You are commenting using your Facebook account. Log Out / Change )

Google+ photo

You are commenting using your Google+ account. Log Out / Change )

Connecting to %s