Lehrstuhl für Biotechnologie und Biophysik

    Priv.-Doz. Dr. Hannes Neuweiler

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    Since 2010Lecturer & 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
    2003–2004Postdoctoral Researcher, Department of Biophysical Chemistry, University of Heidelberg, Germany
    1999–2002 PhD, Department of Physical Chemistry, University of Heidelberg, Germany
    1995–1998Study of Chemistry and Diploma, University of Heidelberg, Germany
    1993–1995Study of Chemistry, University of Frankfurt/Main, Germany
    Protein Engineering & Dynamics

    How does nature succeed in creating a diverse world of complex architectures and sophisticated molecular machines from just linear chains of amino acids? We are seeking to find answers to this question…

    The linear chains of amino acids are called proteins and act as folded structures or intrinsically disordered entities to carry out critical functions in virtually all aspects of life. Protein functional diversity ranges from solid material over motility to biochemical catalysis and signalling. The 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 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 a result of distinct 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, involved in disease states, or that are implicated in material science. Protein engineering is applied to introduce high-resolution fluorescence probes tailored to 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.

    Selected references:

    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. Pressemitteilung.

    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.

    Kontakt
    Biotechnologie & Biophysik
    Biozentrum
    Am Hubland
    97074 Würzburg

    Tel.: +49 931 31-84507
    Fax: +49 931 31-84509

    Suche Ansprechpartner
    Hubland Süd Hubland Nord Campus Dallenberg Fabrikschleichach Humangenetik Campus Medizin