Berlin 2018 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 11: Bioimaging and Biopspectroscopy I
BP 11.10: Vortrag
Dienstag, 13. März 2018, 12:15–12:30, H 1028
Simulation of FRET Dyes Allows Direct Comparison Against Experimental Data — •Ines Reinartz1, Claude Sinner1, and Alexander Schug1,2 — 1Karlsruhe Institute of Technology, Karlsruhe, Germany — 2John von Neumann Institute for Computing, Forschungszentrum Jülich, Jülich, Germany
Single molecule Förster Resonance Energy Transfer (smFRET) experiments provide valuable insight into protein dynamics. Akin to a molecular ruler, different protein conformations can be observed by measuring the energy transfer depending on the distance between selected residues labeled with dyes. Besides this distance, the energy transfer is also dependent on the mutual orientation of the dyes. Both can be gained from atomistic simulations.
We develop a coarse-grained simulation technique with few parameters while maintaining full protein flexibility and including all heavy atoms. The computational efficiency of these simulation protocols allows for simulating large systems and heterogeneous ensembles as found in, e.g., protein folding.
The FRET efficiency histograms we gain from our simulations are directly comparable to experimental measurements. With access to distances and orientations from atomically resolved trajectories, we want to improve the planning and interpretation of smFRET measurements. As an example, we compare distributions from 2-color and 3-color FRET experiments and simulations for ClyA in monomer and protomer conformation, as well as folded and unfolded ensembles of different systems.