Cluster of Excellence –
University of Freiburg

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:

  • 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.
  • Using three-color single-molecule FRET to study the correlation of protein interactions.
    Götz M, Wortmann P, Schmid S, Hugel, T (2018).
    J. Vis. Exp. 131, e56896.
  • 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.
  • The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.
    Jahn M, Rehn A, Pelz B, Hellenkamp B, Richter K, Rief M, Buchner J, Hugel T (2014).
    Proc Natl Acad Sci U S A. 111(50):17881-6
  • 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
  • Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.
    Ratzke C, Mickler M, Hellenkamp B, Buchner J, Hugel T (2010).
    Proc Natl Acad Sci U S A. 107(37):16101-6.
  • 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.