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SUMMARY:LILBID-mass spectrometry: interrogating non-covalent complexes - N
 ina Morgner\, nstitute of physical and theoretical chemistry\, Goethe Univ
 ersity Frankfurt
DTSTART:20170607T093000Z
DTEND:20170607T103000Z
UID:TALK72990@talks.cam.ac.uk
CONTACT:Priyanka Joshi
DESCRIPTION:In recent years LILBID mass spectrometry has been shown to hav
 e great potential for the investigation of biomolecules and biomolecular c
 omplexes that have proven challenging to investigate by more standardly us
 ed methods. The ionization method is soft\, sensitive and tolerant against
  solution additions\, allowing for the investigation of many different kin
 ds of non-covalently bound complexes including soluble or membrane protein
 s as well as RNA/DNA. \n\nFor LILBID-MS micro droplets (30μm diameter) of
  the aqueous analyte solution are generated by a droplet generator at a fr
 equency of 10Hz and transferred to vacuum. There the droplets are irradiat
 ed by an infrared laser pulse\, which deposits its energy into the OH stre
 tching vibrations of the water molecules. This leads to the explosive expa
 nsion of the droplets\, setting the solvated ions free\, which can then be
  analysed. \nVia the laser energy deposited into the droplet the degree of
  complex dissociation can be controlled allowing for the investigation of 
 intact non-covalently bound protein complexes or their building blocks.\n\
 nI will give an overview over recent progress in different areas. We can i
 nvestigate challenging soluble proteins\, as the Alzheimer triggering Aß4
 2 peptide\, for which LILBID allows to follow the aggregation process for 
 Oligomers up to 20mers. We have as well analysed large membrane protein co
 mplexes such as ATPases from detergent micelles. I will introduce the deve
 lopments allowing for the investigation of membrane complexes from nanodis
 cs\, which mimic the proteins native surrounding of the membrane\, where d
 etergent micelles can’t be used satisfactorily. Using this method we cou
 ld for example shed light on the process which leads in cell free expressi
 on systems to the integration of the proteins into the nanodiscs. 
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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