“Our paper describes, for the first time, the high-resolution structure of a protein-conducting channel.”

Our paper describes, for the first time, the high-resolution structure of a protein-conducting channel. Such a structure allows testing of previously reported biochemical data and hypotheses, and provides the basis for the design of future experiments.

The new discovery is the high-resolution structure of this important protein complex, which is present in all cells (including human) and has been conserved throughout evolution. The methodology (X-ray crystallography) is not new.

All cells and cellular organelles are surrounded by lipid membranes, which form a physical barrier. New proteins are synthesized in one location (the cytoplasm), and many of them have to be transported across the membrane barrier to other locations. In addition, newly made membrane proteins have to be inserted into the lipid membrane, where they perform their functions. Both of these tasks, which are essential for all cells, are performed by the protein-conducting channel. Our paper describes the structure of this membrane protein, thus providing, for the first time, direct information as to how this channel works.

My interests and background are in the field of structural biology. Structure determination of membrane proteins is an important and a particularly challenging problem in this field. This project allowed me to learn X-ray crystallography and to work on membrane protein purification in a scientifically stimulating setting. This project has also been a tremendous help for me in securing my current position as a tenure-track Assistant Professor at the University of Massachusetts Medical School Program in Molecular Medicine.