|Since 2010||Lecturer & Group Leader, Department of Biotechnology & Biophysics, University of Würzburg, Germany|
|2006–2010||Marie Curie Fellow (6th framework programme of the EU) and Career Development Fellow in the laboratory of Prof. Alan Fersht, Medical Research Council Centre for Protein Engineering, Cambridge, United Kingdom|
|2004–2006||Postdoctoral Researcher, Department of Applied Laser Physics & Laser Spectroscopy, University of Bielefeld, Germany|
|2003–2004||Postdoctoral Researcher, Department of Biophysical Chemistry, University of Heidelberg, Germany|
|1999–2002||PhD, Department of Physical Chemistry, University of Heidelberg, Germany|
|1995–1998||Study of Chemistry and Diploma, University of Heidelberg, Germany|
|1993–1995||Study of Chemistry, University of Frankfurt/Main, Germany|
How does nature succeed in creating our diverse world of complex protein architectures and sophisticated molecular machines from just linear chains of amino acids? We are seeking answers to this question…
Proteins are linear chains of amino acids and act as folded structures or intrinsically disordered entities that carry out critical functions in virtually all aspects of life. Protein functional diversity ranges from macroscopic structure over motility to biochemical catalysis and signalling. Functional diversity is rooted in the astronomical number of possible sequences that the cellular protein synthesis machinery can generate using only 20 different amino acids as building blocks. Evolution selects for function a tiny subset from this tremendous pool of sequences, which transform into uniquely folded structural entities or remain intrinsically disordered. Structural studies deliver an ever-increasing number of atomic-detailed snapshots of proteins deposited in the Protein Data Bank, which provide our current basis for understanding protein function at a molecular level. But recent years witnessed increasing appreciation that dynamic disorder and conformational change are integral part of function. Often, function is the result of specific structural changes that are triggered or modulated by external stimuli. Deciphering protein mechanisms thus requires the observation of conformational change. This task represents a major challenge for current molecular biology and biophysics because spectroscopy that can detect it is rare.
We investigate proteins that are key players in human biology and disease or that are implicated in material science. We apply protein engineering to introduce high-resolution fluorescence probes that uncover conformational motion and to investigate the contribution of individual amino acids to folding and function. We combine modern methods of molecular biology, including recombinant DNA technology, site-directed mutagenesis and heterologous protein expression, with state-of-the-art fluorescence and complementary protein spectroscopy, involving single-molecule methods and kinetics in multidisciplinary approaches.
Jonathan Schubert, Andrea Schulze, Chrisostomos Prodromou & Hannes Neuweiler, Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics, Nat Commun 2021, 12:6964. doi: 10.1038/s41467-021-27286-5
Heiby, J.C., Goretzki, B., Johnson, C.M., Hellmich, U.A., Neuweiler, H.: Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk. Nature Communications. 10, 4378-- (2019). doi: 10.1038/s41467-019-12365-5 Press release Nature Chemistry Blog „Methionine drives tight binding in spider silk“
Rat, C., Heiby, J.C., Bunz, J.P., Neuweiler, H.: Two-step self-assembly of a spider silk molecular clamp.Nature Communications.9,4779-- (2018). doi: 10.1038/s41467-018-07227-5. Press release. Among the 50 most read journal articles.
Andrea Schulze, Gerti Beliu, Dominic A. Helmerich, Jonathan Schubert, Laurence H. Pearl, Chrisostomos Prodromou & Hannes Neuweiler, Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism, Nat. Chem. Biol. 2016, 12, 628-635. doi: 10.1038/nchembio.2111. Cover article. News and Views. Press release.
Julia Ries, Simone Schwarze, Christopher M. Johnson, and Hannes Neuweiler, Microsecond folding and domain motions of a spider silk protein structural switch, J. Am. Chem. Soc. 2014, 136, 17136-17144. JACS Spotlight. ACS Chemical & Engineering News. Spinnenseide in Bewegung.
Simone Schwarze, Fabian U. Zwettler, Christopher M. Johnson & Hannes Neuweiler, The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening, Nat. Commun. 2013, 4:2815.
doi: 10.38/ncomms3815. Neues über Spinnenseide.
Jenifer K. Lum, Hannes Neuweiler*, and Alan R. Fersht*, Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53, J. Am. Chem. Soc. 2012, 134, 1617-1622.
Daniel P. Teufel, Christopher M. Johnson, Jenifer K. Lum & Hannes Neuweiler, Backbone-driven collapse in unfolded protein chains, J. Mol. Biol. 2011, 409, 250-262. Amongst the top-10 most-read journal articles. “Must Read” evaluation on Faculty of 1000.
Mette H. Jensen, Madhav Sukumaran, Christopher M. Johnson, Ingo H. Greger & Hannes Neuweiler, Intrinsic motions in the N-terminal domain of an ionotropic glutamate receptor detected by fluorescence correlation spctroscopy, J. Mol. Biol. 2011, 414, 96-105.
Hannes Neuweiler, Wiktor Banachewicz & Alan R. Fersht, Kinetics of chain motions within a protein folding intermediate, Proc. Natl Acad. Sci. USA 2010, 107, 22106-22110.
Hannes Neuweiler, Christopher M. Johnson & Alan R. Fersht, Direct observation of ultrafast folding and denatured state dynamics in single protein molecules, Proc. Natl Acad. Sci. USA 2009, 106, 18569-18574.