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hybridFRET - deciphering biomolecular structure and dynamics

Total Cost €


EC-Contrib. €






Project "hybridFRET" data sheet

The following table provides information about the project.


Organization address
postcode: 40225

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Germany [DE]
 Project website
 Total cost 2˙499˙457 €
 EC max contribution 2˙499˙457 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-ADG
 Funding Scheme ERC-ADG
 Starting year 2015
 Duration (year-month-day) from 2015-12-01   to  2020-11-30


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

To understand and modulate biological processes, we need their spatiotemporal molecular models. In this project we propose to build these models by a holistic approach. The recent methodological and technical advances in fluorescence spectroscopy and microscopy as well as in multi-scale modelling of complex biochemical systems set the stage to tackle cross-fertilizing challenges in biophysics, biochemistry and cell biology. The applicant proposes to develop a novel integrative platform for a Molecular Fluorescence Microscope (MFM) to achieve ultimate resolution in space (sub-nanometer) and time (picoseconds) for characterizing structure and dynamics of proteins. MFM will combine Multi-parameter Fluorescence Detection with Computational Microscopy (molecular dynamics and coarse grained simulations) in a hybrid approach, first, to derive a complete molecular description of all fluorescence properties of the tailored dyes in proteins (objectives 1 and 2) and, second, to utilize this information in simulations to report on the protein properties (objective 3). In this hybrid approach high precision FRET measurements are the core experimental technique (hybridFRET). The MFM will allow us to tackle the central biophysical question of how intra- and intermolecular domain interactions modulate proteins' overall structure, dynamics, and thus ultimately function (objective 4). In this proposal we will apply MFM to two prototypic proteins of significant medical relevance. The combination with Multi-parameter Fluorescence Image Spectroscopy will exploit the ultimate resolution of the MFM for molecular protein imaging in live cells. To follow and ultimately understand biological processes, we need their spatiotemporal models of the integrative fluorescence spectroscopy platform. Until now, no holistic use of fluorescence spectroscopy for structural modelling of proteins has been reported.


year authors and title journal last update
List of publications.
2017 Thomas-Otavio Peulen, Oleg Opanasyuk, Claus A.M. Seidel
Combining Graphical and Analytical Methods with Molecular Simulations to Analyze Time-resolved FRET-measurements of Labeled Macromolecules Accurately
published pages: 8211-8241, ISSN: 1520-6106, DOI: 10.1021/acs.jpcb.7b03441
The Journal of Physical Chemistry B 121 2019-07-08
2018 Sinan Kilic, Suren Felekyan, Olga Doroshenko, Iuliia Boichenko, Mykola Dimura, Hayk Vardanyan, Louise C. Bryan, Gaurav Arya, Claus A. M. Seidel, Beat Fierz
Single-molecule FRET reveals multiscale chromatin dynamics modulated by HP1α
published pages: , ISSN: 2041-1723, DOI: 10.1038/s41467-017-02619-5
Nature Communications 9/1 2019-07-08
2016 Mykola Dimura, Thomas O Peulen, Christian A Hanke, Aiswaria Prakash, Holger Gohlke, Claus AM Seidel
Quantitative FRET studies and integrative modeling unravel the structure and dynamics of biomolecular systems
published pages: 163-185, ISSN: 0959-440X, DOI: 10.1016/
Current Opinion in Structural Biology 40 2019-07-08
2018 Maksym Tsytlonok, Hugo Sanabria, Yuefeng Wang, Suren Felekyan, Katherina Hemmen, Aaron Phillips, Mi-Kyung Yun, Brett Waddell, Cheon-Gil Park, Sivaraja Vaithiyalingam, Luigi Iconaru, Stephen W. White, Peter Tompa, Claus A. M. Seidel, Richard Kriwacki
Dynamic anticipation by Cdk2/Cyclin A-bound p27 mediates signal integration in cell cycle regulation
published pages: , ISSN: , DOI:
2018 Hugo Sanabria, Dmitro Rodnin, Katherina Hemmen, Thomas Peulen, Suren Felekyan, Mark R. Fleissner, Mykola Dimura, Felix Koberling, Ralf Kühnemuth, Wayne Hubbell, Holger Gohlke, Claus A.M. Seidel
Resolving dynamics and function of transient states in single enzyme molecules
published pages: , ISSN: , DOI:
2018 Alexander Gansen, Suren Felekyan, Ralf Kühnemuth, Kathrin Lehmann, Katalin Tóth, Claus A. M. Seidel, Jörg Langowski
High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes
published pages: , ISSN: 2041-1723, DOI: 10.1038/s41467-018-06758-1
Nature Communications 9/1 2019-03-06
2018 Björn Hellenkamp, Sonja Schmid, Olga Doroshenko, Oleg Opanasyuk, Ralf Kühnemuth, Soheila Rezaei Adariani, Benjamin Ambrose, Mikayel Aznauryan, Anders Barth, Victoria Birkedal, Mark E. Bowen, Hongtao Chen, Thorben Cordes, Tobias Eilert, Carel Fijen, Christian Gebhardt, Markus Götz, Giorgos Gouridis, Enrico Gratton, Taekjip Ha, Pengyu Hao, Christian A. Hanke, Andreas Hartmann, Jelle Hendrix, Lasse L. Hildebrandt, Verena Hirschfeld, Johannes Hohlbein, Boyang Hua, Christian G. Hübner, Eleni Kallis, Achillefs N. Kapanidis, Jae-Yeol Kim, Georg Krainer, Don C. Lamb, Nam Ki Lee, Edward A. Lemke, Brié Levesque, Marcia Levitus, James J. McCann, Nikolaus Naredi-Rainer, Daniel Nettels, Thuy Ngo, Ruoyi Qiu, Nicole C. Robb, Carlheinz Röcker, Hugo Sanabria, Michael Schlierf, Tim Schröder, Benjamin Schuler, Henning Seidel, Lisa Streit, Johann Thurn, Philip Tinnefeld, Swati Tyagi, Niels Vandenberk, Andrés Manuel Vera, Keith R. Weninger, Bettina Wünsch, Inna S. Yanez-Orozco, Jens Michaelis, Claus A. M. Seidel, Timothy D. Craggs, Thorsten Hugel
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
published pages: 669-676, ISSN: 1548-7091, DOI: 10.1038/s41592-018-0085-0
Nature Methods 15/9 2019-03-06

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