Prof. Dr. Thorsten Hugel

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:

• A blind benchmark of analysis tools to infer kinetic rate constants from single-molecule FRET trajectories.
  Götz M, Barth A, Bohr SS, Börner R, Chen J, Cordes T, Erie DA, Gebhardt C, Hadzic MCAS, Hamilton GL, Hatzakis NS, Hugel T, Kisley L, Lamb DC, de Lannoy C, Mahn C, Dunukara D, de Ridder D, Sanabria H, Schimpf J, Seidel CAM, Sigel RKO, Sletfjerding MB, Thomsen J, Vollmar L, Wanninger S, Weninger KR, Xu P, Schmid S.
  Nat Commun. 2022 Sep 14;13(1):5402.
• Angle-dependent strength of a single chemical bond by stereographic force spectroscopy.
  Cai W, Bullerjahn JT, Lallemang M, Kroy K, Balzer BN, Hugel T.
  Chem Sci. 2022 Apr 26;13(19):5734-5740.
• 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)
  arXiv, arxiv.org/abs/2110.10483.
• 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.
• 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.
• 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.