I am investigating different areas within membrane protein structure and the process of membrane protein folding. One of these is areas is kinks, which are common in alpha-helical transmembrane proteins. A kink is a site where an alpha helix changes direction, and kinks are thought to be important for flexibility and function. Therefore I have investigated their conservation across families of homologous proteins. A major focus in this work was the superfamily of G-protein coupled receptors, which are very important drug targets.
I am now particularly interested in membrane protein folding, from the perspective of insertion into the membrane during translation. One way to learn more about the folding process is through testing our ability to predict protein structures, and therefore I am looking at how knowledge of co-translational folding can improve structure prediction of membrane proteins. Co-translational approaches have been used in protein structure prediction of soluble proteins, but current de novo membrane protein structure prediction methods do not consider the direction of translation in their protocols.