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Structural techniques and single-molecule fluorescence imaging for studying proteins and protein complexes that regulate gene expression
How do the molecular structures and dynamics of these proteins together enable their function? Research efforts in the Deindl Lab are aimed at addressing this question using a combination of single-molecule fluorescence imaging approaches, structural techniques (primarily X-ray crystallography), biochemistry and computer simulations.

Knowledge of the static architecture of proteins and protein complexes alone may not satisfactorily explain how they work. They are inherently dynamic and the time-dependent fluctuations in their structures are often key to their function.
In order to investigate this dynamic nature, we explore single-molecule fluorescence imaging approaches to directly study proteins at work in real time. Their complex dynamics can be difficult to capture in classical bulk experiments since ensemble averaging can obscure the presence of multiple kinetic pathways or transient states. Investigations at the single-molecule level, however, can allow us to directly observe these processes and to correlate structural dynamics with function.

We hope to combine real-time dynamic information from these single-molecule experiments with biochemical and structural data in order to create movies of the proteins and protein complexes at work that provide a quantitative and mechanistic understanding of how they work.