Centre for Biological Signalling Studies

Prof. Dr. Thorsten Hugel

Prof. Dr. Thorsten Hugel

Institute of Physical Chemistry
University of Freiburg

+49 761 203 6192

We use single molecule methods to investigate molecular machines and signaling in biological systems. We focus on understanding complex dynamic biological processes in and out of equilibrium. In addition, we probe the interaction between proteins and lipid bilayers. The core methods are single molecule multi-colour FRET and single molecule force spectroscopy.


10 selected publications:

  • Nanosecond structural dynamics of the chaperone Hsp90
    Sohmen B, Beck C, Seydel T, Hoffmann I, Hermann B, Nüesch M, Grimaldo M, Schreiber F, Wolf S, Roosen-RungeF, Hugel T (2021)
  • Hierarchical dynamics in allostery following ATP hydrolysis monitored by single molecule FRET measurements and MD simulations.
    Wolf S, Sohmen B, Hellenkamp B, Thurn J, Stock G, Hugel T (2021).
    Chem Sci. 12(9):3350-3359.
  • Controlling protein function by fine-tuning conformational flexibility.
    Schmid S, Hugel T (2020).
    Elife. 9:e57180.
  • Conformational dynamics of a single protein monitored for 24 h at video rate.
    Ye W, Götz M, Celiksoy S, Tüting L, Ratzke C, Prasad J, Ricken J, Wegner S V, Ahijado-Guzmán R, Hugel T* and Sönnichsen C* (2018).
    Nanoletters. 18(10):6633-6637
  • Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study.
    Hellenkamp B, Schmid S, et int., Hugel T (2018).
    Nat Methods. 15, 669.
  • Multidomain structure and correlated dynamics determined by self-consistent FRET networks.
    Hellenkamp B, Wortmann P, Kandzia F, Zacharias M, Hugel T (2017).
    Nat Methods. 14(2):174-180.
  • Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments.
    Jahn M, Buchner J, Hugel T, Rief M (2016).
    Proc Natl Acad Sci U S A. 113(5):1232-7.
  • Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery.
    Ratzke C, Hellenkamp B, Hugel T (2014).
    Nat Commun. 5:4192.
  • Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations.
    Ratzke C, Berkemeier F, Hugel T (2012).
    Proc Natl Acad Sci U S A. 109(1):161-6
  • The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.
    Mickler M, Hessling M, Ratzke C, Buchner J, Hugel T (2009).
    Nat Struct Mol Biol.16(3):281-6.