I arrived late last night from Cambridge, UK. After a quick (well 15-hour) taxi, train, tube, plane and another taxi ride…I had arrived to wonderfully snow glistened Philadelphia! Having been awake for almost 22 hours, I fell asleep straight away and right on jet lag cue woke up ready for the day… at 2am. Ouch!
My first day at the conference has been brilliant… and highly caffeinated. I’ve attended talks from sessions: ‘Protein Conformation’, ‘Membrane Transporters & Exchangers I’, ‘The Future of Biophysics’, ‘ Communicating Science’ and ‘New and Notable’. I’m not going to elaborate in detail about each talk, although many were very interesting, instead in homage to tonights Super Bowl XLVII game, which I have come to realise how big of a deal it is here, I thought I would choose two of my favourite talks; one from Baltimore and one from San Francisco, representing the Baltimore Ravens and the San Francisco 49ers! Here goes…
Representing the Baltimore Ravens, we have Anniesha Hack from Johns Hopkins University in Baltimore. Anniesha spoke of her research that involved conducting genetic mutations on the NHE6 and NHE9 gene, which are linked to neurological disorders that include autism. Her group created single nucleotide mutations in NHE9 and combined them with homology modeling and evolutionary analysis in an attempt to decipher the disease-causing mutations. They picked three variants to further investigate; first in yeast systems and later in mouse primary astrocytes. Their results, which revealed a loss of function phenotype for all three mutations, provide a cellular assessment for NHE9 mutations in autism, with the future hope to phenotype screen children at a younger age.
And for the San Francisco 49ers, I chose Michael Lin from Stanford University from my favourite session today, ‘New and Notable’. He spoke about Fluorescent Light induced Proteins (FliP) that involves ‘re-purposing’ photoactive proteins and investigating their function within the cell, or as he put it ‘remote control biology’. His group took the fluorescent Dronpa protein and re-purposed it by attaching a protein of interest. Dronpa, naturally a tetramer, when illuminated at 500 nm (cyan light) breaks down and is no longer fluorescent. The protein of interest, in their case a protease, is no longer ‘caged’ and therefore is free to function. What’s more, the design is generalizable and their group is looking into developing methods for controlling protein function with drugs.
Pretty cool stuff… Thank you Biophysical Society for an excellent day. Now, time for chicken wings and pretending to understand this confusing game! I will leave you with many fascinating (and geeky) Super Bowl facts courtesy of UK’s very own Greg Foot (@gregfoot). http://www.youtube.com/watch?v=HIQYBxE5C_M&feature=youtu.be
Stay tuned for my blogs on ‘Communicating Science’ and ‘The XX files – Women in Biophysics’.