This release is available in German.
Interactions between proteins are of fundamental importance for a number of processes in virtually every living cell. However, in order for the proteins to carry out any biological function, they must first assume their specific three-dimensional shape. A number of reactions have been described in recent years, where one of the interaction partners does not assume its active structure until the actual binding process commences. It was still a great mystery, though, how the binding partners could actually recognize such unstructured proteins.
Scientists led by Professor Thomas Kiefhaber (TUM) posed the question of whether local properties are sufficient for the recognition to take place or whether the unstructured binding partner first had to assume a specific spatial structure. Possible candidates were regularly structural elements such as coiled α-helices or β-pleated sheets, in which internal hydrogen bonds are formed.
In collaboration with Professor Gunter Fischer's research group at the Max Planck Research Unit for Enzymology of Protein Folding Halle/Saale, the scientists developed a novel method for observing the formation of individual hydrogen bonds in the course of a binding process.
The model system was the enzyme ribonuclease S, which in its active form comprises the S-protein and an α-helical S-peptide. While the S-protein has a defined three-dimensional shape, the S-peptide on its own is initially unfolded. The scientists attempted to determine whether the S-protein recognizes the unstructured S-peptide or a small fraction of peptide molecules in their helical conformation. To this end, the oxygen atoms in the peptide bonds were replaced by sulfur atoms via chemical protein synthesis, causing individual hydrogen bonds to become destabilized.
|Contact: Dr. Andreas Battenberg|
Technische Universitaet Muenchen