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My research in the Oxford Protein Informatics Group (OPIG) focuses on kinks in protein helices. These are an important structural feature of proteins, but are not well understood. They occur frequently in membrane proteins, which are a poorly understood class of proteins. Although memebrane proteins are incredibly important in the body, and make up the majority of drug targets, there is a very limited amount of structural data. This is because finding the structure of membrane proteins is much more difficult than finding the structure of other proteins.

Kinks occur in the alpha helices of many proteins, for example ion-channels and GPCRs. Although there have been many studies into kinks, they disagree on where and why kinks occur. The amino acid Proline is frequently found in kinks. However, despite numerous suggestions, no other amino acid plays a clear role in kinks. The contrasting conclusions of the studies is, in part, due to the different methods used to identify kinks. There is no strict definition of a kink, and the distinction between kinked and non-kinked helices is not simple (if you do not believe me, try for yourself here!). As a result, the first part of my doctoral research focused on the many ways to identify kinks.

I am part of the Oxford Protein Informatics Group (OPIG), which is led by my supervisor, Charlotte M. Deane. I am also supervised by Jiye Shi (UCB).

In association with JP Ebejer and Bernhard Knapp, I am currently running a crowd sourcing experiment for my research. It takes about 15 minutes, and requires no specialist knowledge. Click here to participate!

Publications

Kinks are equally prevalent in soluble and membrane proteins. Henry R. Wilman, Jiye Shi, Charlotte M. Deane. Proteins 2014, In Press.

Talks and Posters

Kinks in Membrane Protein Helices - oral presentation at 3Dsig2012, Long Beach, CA

Statistical Approaches to Kinked Helices - Poster presentation at ISMB2013, Berlin

Kinks in Membrane Protein Helices - Poster presentation at ISMB2012, Long Beach, CA