Prof. Dr. Matthias Preller
Institute for Biophysical Chemistry, OE4350
Hannover Medical School
Centre for Structural Systems Biology (CSSB)
German Electron Synchrotron (DESY)
Phone (+49) 511 532 2804
Fax (+49) 511 532 5966
Our research focuses on understanding the functions and roles of different proteins during disease development and to specifically design new means to counteract these particular processes. Key to our work is the combination of computational calculations and simulations with experimental methods to rationalize and decipher the underlying molecular and dynamic processes. Therefore, we apply diverse, interdisciplinary methods, including X-ray crystallographic analysis of proteins and protein-ligand complexes, computer-aided drug design, chemical synthesis of small molecule protein modulators, biophysical binding and activity assays, and computational and structural bioinformatics techniques to explore the binding behavior, mechanisms of action, and the function of the target proteins, respectively.
Current work includes:
The analysis and rational, computer-aided development of small molecule modulators to target genetic and infection diseases in a controlled manner. A particular focus lies here on the design, establisment of synthetic routes and mechanistic investigation of small molecule inhibitors of apicomplexan parasites, including the infection with the malaria parasite.
Deciphering molecular mechanisms and allosteric coupling in molecular motors. Mechanical work and directed movement is crucial for various biological processes. In the cell, directed motion is mostly conducted by molecular motor proteins. However, our knowledge about the molecular events of chemomechanical coupling and transduction remains incomplete. We aim to shed light on allosteric communication pathways within the motor proteins and the mechanisms underlying force production and movement.
Understanding disease development triggered by mutations at the atomic level. The consequences of such disease-related mutations can be diverse, however, many of them affect the structure and conformational dynamics, and thereby the function of the proteins. We are combining computational simulations and biophysical methods to unravel the effects of the mutations on the protein function, structure, and dynamics.