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SUMMARY:Thermostabilisation of G protein-coupled receptors to facilitate s
 tructure determination - Chris Tate\, MRC Laboratory of Molecular Biology
DTSTART:20150422T131500Z
DTEND:20150422T141500Z
UID:TALK57070@talks.cam.ac.uk
CONTACT:Lucy Colwell
DESCRIPTION:A prerequisite for the crystallisation of integral membrane pr
 oteins is that the purified protein must be stable in detergent solution. 
 Unfortunately\, many therapeutically relevant membrane proteins are very u
 nstable upon detergent solubilisation and they are therefore difficult to 
 purify and crystallise. We have developed a simple strategy for the thermo
 stabilisation of membrane proteins based on scanning mutagenesis coupled t
 o ligand-based thermostability assays. I will discuss this methodology\, h
 ow this has helped structure determination and a few of the highlights of 
 the structures determined. In addition\, I will discuss what we have learn
 t about factors that affect the thermostability of a G protein-coupled rec
 eptor and how well we can predict these mutations computationally. 
LOCATION:Department of Chemistry\, Cambridge\, Pfizer lecture theatre
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