The research group was headed by Prof. Dr. Ulrich H. E. Hansmann from 1st of July 2005 to 30th of June 2008. Many thanks to all group members for the successful work over these three years! Information on Prof. Dr. Hansmann's ongoing work can be found here.

Over the last few decades, high-performance computing has extended the range of phenomena that can be investigated within the framework of physics. One example is biology where supercomputers have become a crucial tool in the deciphering of whole genomes, the characterization of their encoded proteins, and the study of function, mutual interaction and regulation of these proteins. Modeling biological system is one of the defining challenges in computational science requiring both new hardware and novel methods. Within the emerging field of computational biology and biophysics our research focuses on the physics of proteins, "nanomachines" that are responsible for transporting molecules, catalyzing biochemical reactions in the cell, or fighting infections. As the function of a protein is a direct consequence of its three-dimensional structure we are interested to explore how these structures emerge from the protein's chemical composition (the sequence of amino acids as specified in the genome). A detailed knowledge of this folding process could lead to a deeper understanding of various diseases that are caused by the mis-folding of proteins, or enable the design of novel drugs with customized properties.

Tackling this protein folding problem on a computer is a notoriously difficult problem and one aim of the research in our group. In particular we have developed and adapted novel algorithms such as multicanonical sampling and energy landscape paving that are instrumental in performing our research on:

• the sequence-structure relationship of proteins i.e. the prediction of the three-dimensional structure of a protein from its amino acid sequence. Here are our results from the recent CASP 7 competition of protein structure prediction methods.
• the folding mechanism of proteins with a special emphasis on the conditions under which they mis-fold and aggregate (a cause of several neurological disorders).

We will now test our methods on a range of new topics including:

• Protein-Ligand interactions for aiding in rational drug design.
• Protein-Interaction networks to unravel cellular signaling.
• Protein-Nanotube interactions for applications in nanoscale electronics.

As several topics have direct applications we are constantly looking to extend our international network of collaborations.