Associate Prof Maike Bublitz

Associate Prof Maike Bublitz


Our research aims at understanding, how the biological function of membrane transport proteins is encoded in their 3D structure

Associate Prof Maike Bublitz

Molecular Mechanisms of Membrane Transport Processes

The plasma membrane of all living cells acts as a barrier between the cell’s contents and the “outside world”. Defined concentration gradients across the plasma membrane are constantly generated and maintained by certain membrane transport proteins, while others exploit the energy stored in such gradients for so-called secondary transport processes.


Our main focus lies on primary active transport proteins from the P-type ATPase family. P-type ATPases are large, highly flexible transporters that use energy from ATP for the specific transport of ions across cellular membranes. We are particularly interested in the ATPase with the smallest substrate of all, the H?-ATPase – or proton pump.


It pumps single protons across the plasma membrane in plants and fungi and thereby creates the proton-motive force, which is vital for the organism i.e. by fuelling nutrient uptake systems. Using a variety of state-of-the-art biochemical and biophysical methods, we want to thoroughly characterise the proton transport process and its regulation in vitro, and by determining a high-resolution crystal structure of the proton pump, we aim at understanding the structural basis for the specific and unidirectional transport of protons across the membrane. This research also provides an important framework for the development of novel antifungal medication.


Furthermore, we are exploring and developing new methods for investigating membrane protein-lipid interactions and determining structures from small and/or poorly diffracting crystals.


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