Predicting the structure of protein assemblies
Many biological processes are controlled by large multi-component protein assemblies, the size and complexity of which typically precludes the determination of their high-resolution structures. Yet, for these systems ample non-structural data is typically available providing a wealth of lower resolution information. Our goal is to use high-resolution structural modeling techniques guided by constraints taken from lower resolution experimental data to generate structural models of important biological protein assemblies for which high resolution structural determination is unfeasible. In particular, we are interested in a subclass of protein assemblies, homomeric assemblies, which are produced by the repetition of single type of subunit. Homomeric assemblies typically adopt internal symmetry, which provides a crucial constraint in the molecular modeling. For more information, click here.
Designing the structure of protein assemblies
Achievement of rational control of protein structure and function has been a longstanding goal in protein science. Realization of this goal would have transformative implications on several disciplines of science: biochemistry, molecular biology, biomedicine, biotechnology and nanotechnology. In addition to paving the way for the development of a range of functional biomolecules - from protein drugs to enzymes and biomaterials - it would also refine and extend the understanding of the fundamental determinants of protein structure formation. We develop computational methods to design novel protein assemblies and to control the assembly structure formation at high precision. We use the designed assemblies as model system to understand protein assembly formation and the evolution of protein complexes as well as to design functional proteins for use in biotechnology and nanotechnology. For more information, click here.
Computational method development with Rosetta
Together with a large number of research groups in various countries we develop the macromolecular modeling suite Rosetta. For more information, visit the Rosetta Commons website.
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