Jörg Fitter Forschungszentrum Jülich, Institute of Complex Systems ICS-5, Germany, Germany,
1 protocol

Michele Cerminara Institute of Complex Systems ICS-5, Forschungszentrum Jülich, Germany, Germany,
1 protocol

Mayuri Sadoine Forschungszentrum Jülich, Institute of Complex Systems ICS-5, Germany, Germany,
1 protocol

Alexandros Katranidis
  • Forschungszentrum Jülich, Institute of Complex Systems ICS-5, Germany, Germany,
  • 1 Author merit


Ph.D in Nanobiotechnology, Aristotle University of Thessaloniki, Greece, 2009

Current position

Project leader, Institute of Complex Systems ICS-5, Research Center Juelich, Germany

Publications (since 2009)

  1. Sadoine, M., Cerminara, M., Gerrits, M., Fitter, J. and Katranidis, A. (2018). Cotranslational Incorporation into Proteins of a Fluorophore Suitable for smFRET Studies. ACS Synth Biol 7(2): 405-411.
  2. Sadoine, M., Cerminara, M., Kempf, N., Gerrits, M., Fitter, J. and Katranidis, A. (2017). Selective Double-Labeling of Cell-Free Synthesized Proteins for More Accurate smFRET Studies. Anal Chem 89(21): 11278-11285.
  3. Wruck, F., Katranidis, A., Nierhaus, K. H., Buldt, G. and Hegner, M. (2017). Translation and folding of single proteins in real time. Proc Natl Acad Sci U S A 114(22): E4399-E4407.
  4. Kempf, N., Remes, C., Ledesch, R., Zuchner, T., Hofig, H., Ritter, I., Katranidis, A. and Fitter, J. (2017). A Novel Method to Evaluate Ribosomal Performance in Cell-Free Protein Synthesis Systems. Sci Rep 7: 46753.
  5. Tang, Y., Dai, L., Zhang, X., Li, J., Hendriks, J., Fan, X., Gruteser, N., Meisenberg, A., Baumann, A., Katranidis, A. and Gensch, T. (2015). SNSMIL, a real-time single molecule identification and localization algorithm for super-resolution fluorescence microscopy. Sci Rep 5: 11073.
  6. Gabba, M., Poblete, S., Rosenkranz, T., Katranidis, A., Kempe, D., Zuchner, T., Winkler, R. G., Gompper, G. and Fitter, J. (2014). Conformational state distributions and catalytically relevant dynamics of a hinge-bending enzyme studied by single-molecule FRET and a coarse-grained simulation. Biophys J 107(8): 1913-1923.
  7. Lamprou, P., Kempe, D., Katranidis, A., Buldt, G. and Fitter, J. (2014). Nanosecond dynamics of calmodulin and ribosome-bound nascent chains studied by time-resolved fluorescence anisotropy. Chembiochem 15(7): 977-985.
  8. Katranidis, A., Grange, W., Schlesinger, R., Choli-Papadopoulou, T., Bruggemann, D., Hegner, M. and Buldt, G. (2011). Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers. FEBS Lett 585(12): 1859-1863.
  9. Katranidis, A., Melachroinos, A., Karagiannidis, P.G., Lousinian, S., Papadopoulos, G., Logothetidis, S. and Choli-Papadopoulou, T. (2011) Biofunctionalization of PET/SiO2 surfaces for single molecule experiments and medical applications. NANO 6 271–277.
  10. Fitter, J., Katranidis,  A., Rosenkranz, T., Atta, D., Schlesinger, R. and Büldt,  G. (2011) Single molecule fluorescence spectroscopy: A tool for protein studies approaching cellular environmental conditions. Soft Matter 7, 1254-1259.
  11. Rosenkranz, T., Katranidis, A., Atta, D., Gregor, I., Enderlein, J., Grzelakowski, M., Rigler, P., Meier, W. and Fitter, J. (2009). Observing proteins as single molecules encapsulated in surface-tethered polymeric nanocontainers. Chembiochem 10(4): 702-709.
  12. Katranidis, A., Atta, D., Schlesinger, R., Nierhaus, K. H., Choli-Papadopoulou, T., Gregor, I., Gerrits, M., Buldt, G. and Fitter, J. (2009). Fast biosynthesis of GFP molecules: a single-molecule fluorescence study. Angew Chem Int Ed Engl 48(10): 1758-1761.
1 Protocol published
Preparation of Cell-free Synthesized Proteins Selectively Double Labeled for Single-molecule FRET Studies
Authors:  Mayuri Sadoine, Michele Cerminara, Jörg Fitter and Alexandros Katranidis, date: 06/20/2018, view: 421, Q&A: 0
Single-molecule FRET (smFRET) is a powerful tool to investigate molecular structures and conformational changes of biological molecules. The technique requires protein samples that are site-specifically equipped with a pair of donor and acceptor ...