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SUMMARY:Membrane proteins - the lipid connection - Carol Robinson\, univer
 sity of Oxford
DTSTART:20170307T110000Z
DTEND:20170307T120000Z
UID:TALK70281@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The realisation that the lipid environment is crucial for main
 taining the structure and function of membrane proteins prompts new method
 s to understand lipid interactions. One such method\, mass spectrometry\, 
 is emerging with the potential to monitor different modes of lipid binding
  to membrane protein complexes. Initial studies monitored the addition of 
 lipids and deduced the kinetic and thermodynamic effects of lipid binding 
 to proteins. Recently however\, we have focused on identifying lipids alre
 ady present\, explicitly in plugs\, annular rings or cavities. Lipids that
  bind within these orifices to membrane proteins will have higher residenc
 e times than those in the bulk lipid bilayer and consequently can be quant
 ified and characterized by mass spectrometry. In special cases\, lipids id
 entified within cavities have been proposed as substrates following activi
 ty assays. Alternatively\, a gas phase unfolding protocol can be used to d
 istinguish lipids that are important for stability. In this lecture I will
  provide an overview of recent advances in mass spectrometry\, with a part
 icular focus on the distinction of the various modes of lipid binding\, th
 eir implications for structure and function\, as well as new directions th
 at lie ahead. 
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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