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BP: Fachverband Biologische Physik
BP 28: Single Molecule Biophysics
BP 28.1: Vortrag
Donnerstag, 15. März 2018, 09:30–09:45, H 1058
Cell free protein synthesis systems and single molecule fluorescence studies: a perfect marriage — Alexandros Katranidis1, Mayuri Sadoine1, Noemie Kempf1, Michael Gerrits2, Michele Cerminara1, and •Jörg Fitter1,3 — 1Research Centre Juelich, ICS-5, Juelich, Germany — 2TU Berlin, Biocatalysis Group, Department of Chemistry, Berlin, Germany — 3RWTH Aachen University, I. Physikalisches Institut (IA), AG Biophysik, Aachen, Germany
Protein synthesis is a fundamental cellular process, by which ribosomes decode genetic information and convert it into an amino acid sequence. This highly complex process does not necessarily require cell integrity, but can also proceed in so called cell-free protein systems. This opens the door for comprehensive studies to obtain a deeper understanding of individual steps of the translation cycle and of the folding of de novo synthesized proteins. The use of cell-free protein synthesis (CFPS) systems allowed us to watch some of these essential steps in real time and on single molecule level [1,2]. On the other hand the open nature of the CFPS system allows the production of tailor-made protein samples, perfectly suited for single molecule Förster resonance energy transfer (smFRET) studies [3]. Examples from both above mentioned topics will be presented and demonstrate the strength of combining CFPS with single molecule fluorescence studies.
[1] A. Katranidis et al., Angewandte Chemie Int. Edit., 48, 1758-1761, (2009); [2] N. Kempf et al., Sci. Rep., 7, 46753, (2017); [3] M. Sadoine et al., Anal. Chem., 89, 11278-11285, (2017)