Persönlicher Status und Werkzeuge

Prof. Dr. Martin Zacharias



Contact Details

Business card at TUMonline

Academic Career and Research Areas

The research of Prof. Zacharias (b. 1961) focuses on the structure and dynamics of biomolecules. He uses computer simulation methods to study the movement of proteins and nucleic acids imaged with atomic resolution and understand the forces generated. His work also involves creating realistic predictions on the structure formation and association of biomolecules.

After studying at Freie Universität Berlin, Prof. Zacharias did his doctorate there in 1991 in cooperation with the Max Planck Institute for Molecular Genetics. He went on to do postdoctoral research at the University of Houston and the University of Colorado. After that, he completed his lecturer qualification at Humboldt University in Berlin and headed up a research group at Leibniz Institute for Molecular Biotechnology in Jena. He took up a professorship at Jacobs University Bremen prior to accepting his current position of Chair of Biomolecular Dynamics at TUM in 2009.


  • Mitglied „Faculty of 1000“ (2009)
  • Affiliate-Member PNNL (1999)
  • DFG-Habilitationsstipendiat (1996)
  • DFG-Forschungsstipendiat (1992)

Key Publications (all publications)

Zacharias M: “Accounting for conformational changes during protein-protein docking”. Current Opinion Structural Biology. 2010; 20:180-186.


Kannan S, Zacharias M: “Folding simulations of Trp-cage mini protein in explicit solvent using biasing potential replica-exchange molecular dynamics simulations”. Proteins. 2009; 76:448-460.


Curuksu J, Zakrzewska K, Zacharias M: “Magnitude and direction of DNA bending induced by screw-axis orientation: influence of sequence, mismatches and abasic sites”. Nucleic Acids Research. 2008; 36:2268-2283.


Roccatano D, Barthel A, Zacharias M: “Structural flexibility of the nucleosome core particle at atomic resolution studied by molecular dynamics simulation”. Biopolymers. 2007; 85:407-421.


Zacharias M: “Protein-protein docking with a reduced protein model accounting for side-chain flexibility”. Protein Science. 2003; 12:1271-1282.