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Thermostabilisation of G protein-coupled receptors to facilitate structure determination

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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.

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