The Workgroup Protein Interactions at the Ruhr-Universität Bochum investigates mechanisms in the interactions and enzymatic activity of proteins involved in immunity and disease
Human guanylate binding proteins from the family of large GTPases, as well as small GTP binding proteins like the oncogene Ras, employ nucleotide binding and hydrolysis in protein interactions in order to switch between different structural states and to alter the functional status.
Biochemical and biophysical methods help to understand the interplay of these proteins on the molecular level and to relate quantitative characteristics of protein interactions to the biological activity.
Protein interactions: the key agents in living organisms
The interactions of proteins with each other, and with other molecules, as well as with water as solvent and other cosolvents, form the basis of most biological processes. Using biochemical and biophysical techniques, as well as self-developed methods, Workgroup Protein Interactions investigates the interactions between proteins that play an important role in the mediation of cellular signals.
In addition, the Workgroup Protein Interactions investigates molecular processes in the enzymatically catalysed hydrolysis of guanosine triphosphate (GTP), which is important for the control of protein interactions.
On the one hand, our work aims to elucidate the specific mechanisms of action of the examined proteins and, on the other hand, to derive universally valid laws.
In order to study the interactions of proteins of interest, Workgroup Protein Interactions first needs to prepare and purify them. Using a suitable expression vector, the respective protein is synthesised in bacterial cultures and then purified by different chromatographic methods in two or three steps.
Standard molecular biological methods (in particular PCR, polymerase chain reaction) allow the construction of desired variants of the proteins. In particular, the introduction of certain point mutations or the deletion of one or more protein domains, followed by the biophysical studies of the altered properties and the comparison with the wild type allow meaningful conclusions on the functioning of the proteins.