Priv.-Doz. Dr. Hannes Neuweiler | |
Telefon: | +49 931 31-83872 |
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 |
List of publications
2021 [ nach oben ]
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1.Rajab, S., Bismin, L., Schwarze, S., Pinggera, A., Greger, I.H., Neuweiler, H.: Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains. Communications Biology. 4, 1056- (2021).
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2.Schubert, J., Schulze, A., Prodromou, C., Neuweiler, H.: Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics. Nature Communications. 12, 6964- (2021).
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3.Johe, P., Jung, S., Endres, E., Kersten, C., Zimmer, C., Ye, W., Sönnichsen, C., Hellmich, U.A., Sotriffer, C., Schirmeister, T., Neuweiler, H.: Warhead Reactivity Limits the Speed of Inhibition of the Cysteine Protease Rhodesain. ACS Chem. Biol. 16, 661–670 (2021).
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4.Johé, P., Jaenicke, E., Neuweiler, H., Schirmeister, T., Kersten, C., Hellmich, U.A.: Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes. Journal of Biological Chemistry. 296, 100565- (2021).
2020 [ nach oben ]
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1.Goretzki, B., Heiby, J.C., Hacker, C., Neuweiler, H., Hellmich, U.A.: NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis. Biomolecular NMR Assignments. 14, 67–71 (2020).
2019 [ nach oben ]
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1.Banaszek, A., Bumm, T.G.P., Nowotny, B., Geis, M., Jacob, K., Wölfl, M., Trebing, J., Kucka, K., Kouhestani, D., Gogishvili, T., Krenz, B., Lutz, J., Rasche, L., Hönemann, D., Neuweiler, H., Heiby, J.C., Bargou, R.C., Wajant, H., Einsele, H., Riethmüller, G., Stuhler, G.: On-target restoration of a split T cell-engaging antibody for precision immunotherapy. Nature Communications. 10, 5387- (2019).
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2.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).
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3.Mercier, R., Wolmarans, A., Schubert, J., Neuweiler, H., Johnson, J.L., LaPointe, P.: The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. Nature Communications. 10, 1273- (2019).
2018 [ nach oben ]
2017 [ nach oben ]
2016 [ nach oben ]
2015 [ nach oben ]
2014 [ nach oben ]
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1.Ries, J., Schwarze, S., Johnson, C.M., Neuweiler, H.: Microsecond folding and domain motions of a spider silk protein structural switch. Journal of the American Chemical Society. null (2014).
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2.Sauer, M., Neuweiler, H.: PET-FCS: Probing Rapid Structural Fluctuations of Proteins and Nucleic Acids by Single-Molecule Fluorescence Quenching. In: Engelborghs, Y. und Visser, A.J. (hrsg.) Methods Mol Biol - Fluorescence Spectroscopy and Microscopy. S. 597–615. Humana Press (2014).
2013 [ nach oben ]
2012 [ nach oben ]
2011 [ nach oben ]
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1.Jensen, M.H., Sukumaran, M., Johnson, C.M., Greger, I.H., Neuweiler, H.: Intrinsic Motions in the N-Terminal Domain of an Ionotropic Glutamate Receptor Detected by Fluorescence Correlation Spectroscopy. Journal of Molecular Biology. 414, 96–105 (2011).
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2.Teufel, D.P., Johnson, C.M., Lum, J.K., Neuweiler, H.: Backbone-Driven Collapse in Unfolded Protein Chains. Journal of Molecular Biology. 409, 250–262 (2011).
2010 [ nach oben ]
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1.Neuweiler, H., Banachewicz, W., Fersht, A.R.: Kinetics of chain motions within a protein-folding intermediate. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 107, 22106–22110 (2010).
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2.Arbely, E., Rutherford, T.J., Neuweiler, H., Sharpe, T.D., Ferguson, N., Fersht, A.R.: Carboxyl pK(a) Values and Acid Denaturation of BBL. JOURNAL OF MOLECULAR BIOLOGY. 403, 313–327 (2010).
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3.Arbely, E., Neuweiler, H., Sharpe, T.D., Johnson, C.M., Fersht, A.R.: The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces. PROTEIN SCIENCE. 19, 1704–1713 (2010).
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4.Daidone, I., Neuweiler, H., Doose, S., Sauer, M., Smith, J.C.: Hydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains. PLOS COMPUTATIONAL BIOLOGY. 6, (2010).
2009 [ nach oben ]
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1.Neuweiler, H., Sharpe, T.D., Johnson, C.M., Teufel, D.P., Ferguson, N., Fersht, A.R.: Downhill versus Barrier-Limited Folding of BBL 2: Mechanistic Insights from Kinetics of Folding Monitored by Independent Tryptophan Probes. JOURNAL OF MOLECULAR BIOLOGY. 387, 975–985 (2009).
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2.Neuweiler, H., Johnson, C.M., Fersht, A.R.: Direct observation of ultrafast folding and denatured state dynamics in single protein molecules. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 106, 18569–18574 (2009).
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3.Huang, F., Ying, L., Neuweiler, H., Fersht, A.R.: Reply to Campos et al.: Direct observation versus ambiguous kinetics and thermodynamics. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 106, E140 (2009).
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4.Neuweiler, H., Sharpe, T.D., Rutherford, T.J., Johnson, C.M., Allen, M.D., Ferguson, N., Fersht, A.R.: The Folding Mechanism of BBL: Plasticity of Transition-State Structure Observed within an Ultrafast Folding Protein Family. JOURNAL OF MOLECULAR BIOLOGY. 390, 1060–1073 (2009).
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5.Doose, S., Neuweiler, H., Sauer, M.: Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules. CHEMPHYSCHEM. 10, 1389–1398 (2009).
2008 [ nach oben ]
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1.Schuettpelz, M., Schoening, J.C., Doose, S., Neuweiler, H., Peters, E., Staiger, D., Sauer, M.: Changes in conformational dynamics of mRNA upon AtGRP7 binding studied by fluorescence correlation spectroscopy. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. 130, 9507–9513 (2008).
2007 [ nach oben ]
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1.Agaylan, A., Binder, D., Sauer, M., Neuweiler, H., Meyer, O., Kiesewetter, H., Salama, A.: A highly sensitive particle agglutination assay for the detection of P53 autoantibodies in patients with lung cancer. Cancer. 110, 2502–2506 (2007).
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2.Doose, S., Neuweiler, H., Barsch, H., Sauer, M.: Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 104, 17400–17405 (2007).
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3.Neuweiler, H., Lollmann, M., Doose, S., Sauer, M.: Dynamics of unfolded polypeptide chains in crowded environment studied by fluorescence correlation spectroscopy. JOURNAL OF MOLECULAR BIOLOGY. 365, 856–869 (2007).
2006 [ nach oben ]
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1.Kim, J., Doose, S., Neuweiler, H., Sauer, M.: The initial step of DNA hairpin folding: a kinetic analysis using fluorescence correlation spectroscopy. NUCLEIC ACIDS RESEARCH. 34, 2516–2527 (2006).
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2.Schüttpelz, M., Müller, C., Neuweiler, H., Sauer, M.: UV Fluorescence Lifetime Imaging Microscopy: A Label-Free Method for Detection and Quantification of Protein Interactions. Analytical Chemistry. 78, 663–669 (2006).
2005 [ nach oben ]
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1.Scheffler, S., Sauer, M., Neuweiler, H.: Monitoring antibody binding events in homogeneous solution by single-molecule fluorescence spectroscopy. ZEITSCHRIFT FUR PHYSIKALISCHE CHEMIE-INTERNATIONAL JOURNAL OF RESEARCH IN PHYSICAL CHEMISTRY & CHEMICAL PHYSICS. 219, 665–678 (2005).
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2.Neuweiler, H., Doose, S., Sauer, M.: A microscopic view of miniprotein folding: Enhanced folding efficiency through formation of an intermediate. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 102, 16650–16655 (2005).
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3.Neuweiler, H., Sauer, M.: Exploring life by single-molecule fluorescence spectroscopy. ANALYTICAL CHEMISTRY. 77, 178A–185A (2005).
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4.Doose, S., Neuweiler, H., Sauer, M.: A close look at fluorescence quenching of organic dyes by tryptophan. CHEMPHYSCHEM. 6, 2277–2285 (2005).
2004 [ nach oben ]
2003 [ nach oben ]
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1.Neuweiler, H., Schulz, A., Bohmer, M., Enderlein, J., Sauer, M.: Measurement of submicrosecond intramolecular contact formation in peptides at the single-molecule level. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. 125, 5324–5330 (2003).
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2.Vaiana, A., Neuweiler, H., Schulz, A., Wolfrum, J., Sauer, M., Smith, J.: Fluorescence quenching of dyes by tryptophan: Interactions at atomic detail from combination of experiment and computer simulation. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. 125, 14564–14572 (2003).
2002 [ nach oben ]