fivemack (fivemack) wrote,
fivemack
fivemack

No longer in Chicago

That was a fairly intense conference: talks started at eight and finished at five, followed by a two-hour poster session, followed by organised evening events until eleven. I got to wander up the Magnificent Mile and go to the 94th floor of the John Hancock, which gives a nice view of the city - why do so few apartment blocks have rooftop swimming-pools? - but that was all the touristing available. Tiring enough that I managed to sleep on the red-eye, and all four of us were fast asleep in the taxi from Heathrow.

That's the end of the most hectic part of two hectic months; on the other hand we have to get a new release of the software out at the end of September, so I don't get to relax very long.

The Nobel Laureate speeches on the ribosome crystal structure each showed a video in their own unique style of how the ribosome worked. This was absolutely heroic work; it took two decades to get any structures at all, and even though finding the structure of a crystal with contents very similar to one you know already is much easier, the increment to get a structure of a new antibiotic bound to the ribosome is months of crystallisation effort to end up with the positions of maybe fifty atoms. Tom Steitz is looking at taking pairs of antibiotics that bind in nearby places and constructing composite molecules which bind one end at one site and one end at another; Ada Yonath is looking at pairs of antibiotics that bind in different places and suggesting just dosing both at once, which seems to achieve a similar effect at several hundred million dollars less in drug development cost.

There's a lot of rivalry between the groups; Steitz and the third winner Venki Ramakrishnan appeared on the front page of the Stockholm paper with the crown princess sitting between them; Yonath pointed out that she wasn't in that picture because she had been seated with the king, and showed this rather sweet cartoon.

The talk on Raman spectroscopy was fun: I always like hearing about new experimental methods, and this one lets you (sometimes a photon from an intense laser beam gets scattered backwards with its energy reduced by the vibrational energy of some chemical bond, so you focus a laser on the interior of the crystal and measure accurately the spectrum of the light that bounces back, with a notch filter to take the laser itself out) watch the infra-red spectrum of a protein evolve as it does its job: you can observe 'something interesting happens twenty minutes after mixing in the substrate', you can have a good idea of what it is that's happening by looking at the wavelengths, and then you freeze the crystal at the appropriate time and do X-ray diffraction to see exactly where the atoms are as the interesting thing happens. And the group presenting can do this on RNA polymerase, and (after some pretty fearsome experimental issues - you need all-carbon-13, all-nitrogen-15 nucleotide triphosphates to get the bands out of the way of the bands from all the other nucleotides in the template DNA) you can see exactly how the new nucleotides are stuck on the end of the RNA that's forming.
Tags: biochemistry
Subscribe
  • Post a new comment

    Error

    default userpic

    Your IP address will be recorded 

    When you submit the form an invisible reCAPTCHA check will be performed.
    You must follow the Privacy Policy and Google Terms of use.
  • 2 comments