Till Böcking

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Molecular machines –what makes them tick?

To combat viruses, host cells have developed weapons to sabotage the delivery of viral genetic code into their nuclei. There are specialised proteins that either crack open the protective viral capsid prematurely—exposing its genetic material to degradation—or lock the DNA in so it can’t enter the nucleus.

Till Böcking wants to understand how these and other molecular machines work.

By reconstituting these protein interactions—and watching them work using single molecule imaging—Till can see just what is required for the machines to run. He also hopes his findings will help in drug design to improve these machines and fight disease.

We develop fluorescence imaging approaches to visualise the dynamics of self-assembly processes at the single molecule level. The advantage of single molecule measurements is that they can resolve the kinetics of processes without the need for synchronisation and permit the detection of short-lived intermediates in the reaction pathways that are otherwise averaged out in traditional ensemble measurements.

Our work draws on approaches from the physical sciences with development of microfluidic imaging devices, surface chemistry approaches and development of automated image analysis software.

Current projects at Molecular Machines Research page

About Till Böcking

Till is a Senior Lecturer in the Department of Anatomy at UNSW. After undergraduate studies in biochemistry at the University of Bonn in Germany, he trained in the physical sciences at UNSW with Hans Coster (PhD in Biophysics) and with Justin Gooding focusing on molecular self-assembly before heading to Boston to work on the endocytosis machinery with cell biologist Tom Kirchhausen at Harvard Medical School.He now leads the Molecular Machines Group in Single Molecule Science.

Selected Publications

Al-Zyoud, Hynson, Ganuelas, Coster, Duff, Baker, Stewart, Giannoulatou, Ho, Gaus, Liu, Lee, Böcking. Binding of transcription factor GabR to DNA requires recognition of DNA shape at a location distinct from its cognate binding site. Nucleic Acids Research 2016, 44: 1411.

Polling, Ormsby, Wood, Lee, Shoubridge, Hughes, Thomas, Griffin, Hill, Bowden, Böcking, Hatters. Polyalanine expansions drive a shift into alpha-helical clusters without amyloid-fibril formation. Nature Structural & Molecular Biology 2015, 22: 1008.   

Böcking, T., Aguet, F., Rapoport, I., Banzhaf, M., Yu, A., Zeeh, J.-C., & Kirchhausen, T. Key interactions for clathrin coat stability. Structure 2014, 22(6), 819–829. doi.org/10.1016/j.str.2014.04.002

Böcking, T., Aguet, F., Harrison, S. C., & Kirchhausen, T. Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating. Nature Structural & Molecular Biology 2011, 18(3), 295–301. doi.org/10.1038/nsmb.1985

Böcking, T., Kilian, K. A., Reece, P. J., Gaus, K., Gal, M., & Gooding, J. J. Substrate independent assembly of optical structures guided by biomolecular interactions. ACS Applied Materials & Interfaces 2010, 2(11), 3270–3275. doi.org/10.1021/am1007084

Click here for full publication list

More Information

Career Highlights

  • Human Frontiers Science Program Cross-disciplinary Fellowship (2007)
  • ARC Future Fellow (2011)
  • NHMRC Career Development Award, honourary (2011)

Lab Members

  • Miro Janco (Postdoctoral fellow)
  • Tobias Rosenkranz (Postdoctoral fellow)  
  • Vaibhav Shah (Postdoctoral fellow)  
  • James Walsh (Postdoctoral fellow)
  • Chantal Márquez Badilla (PhD student)
  • Ilina Bareja (PhD student)
  • Quill Bowden (PhD student)
  • Derrick Lau (PhD student)
  • Bailey Hao (Honours student)


Chaperone Mechanisms

HIV Host-cell Interactions

Actin Assembly Machines

Single Molecule Approaches

Current Funding Sources

  • Australian Research Council
  • National Health and Medical Research Council
  • Australian Centre for HIV and Hepatitis Virology Research