Thermostabilisation of G protein-coupled receptors to facilitate structure determination

Add to your list(s) Download to your calendar using vCal

• Chris Tate, MRC Laboratory of Molecular Biology
• Wednesday 22 April 2015, 14:15-15:15
• Department of Chemistry, Cambridge, Pfizer lecture theatre.

If you have a question about this talk, please contact Lucy Colwell.

A prerequisite for the crystallisation of integral membrane proteins is that the purified protein must be stable in detergent solution. Unfortunately, many therapeutically relevant membrane proteins are very unstable upon detergent solubilisation and they are therefore difficult to purify and crystallise. We have developed a simple strategy for the thermostabilisation of membrane proteins based on scanning mutagenesis coupled to ligand-based thermostability assays. I will discuss this methodology, how this has helped structure determination and a few of the highlights of the structures determined. In addition, I will discuss what we have learnt about factors that affect the thermostability of a G protein-coupled receptor and how well we can predict these mutations computationally.

This talk is part of the Theory - Chemistry Research Interest Group series.

This talk is included in these lists:

• All Talks (aka the CURE list)
• Cambridge Infectious Diseases
• Department of Chemistry
• Department of Chemistry, Cambridge, Pfizer lecture theatre
• Featured lists
• Lennard-Jones Centre external
• School of Physical Sciences

Note that ex-directory lists are not shown.