We interrogate the role of membrane curvature stress in the aggregation behavior of integral proteins. In particular, we seek to find correlations between the transmembrane shape of proteins and lateral pressure profile of membranes. Using de-novo designed transmembrane proteins of specific shape we tune the lateral pressures by varying the lipid composition of artificial membranes.
To achieve our goals we combine several experimental and computational approaches, including single molecule FRET, SAXS, AFM and MD simulations. Primary collaborators of our project are Gustav Oberdorfer (TU Graz, Austria: protein design), Robert Ernst (Saarland University, Germany: protein expression and purification), and Robert Vácha (CETEIC, Czech Republic: MD simulations).
