Torsten HERRMANN

Research Director CNRS
work phone: 0426233882

Research

The group’s research primarily focuses on the developing of computational methods for the characterization and understanding of the dynamics, interactions, and function of proteins and their complexes at the atomistic level by solution and solid-state nuclear magnetic resonance (NMR) spectroscopy. Yet, we are also actively developing new computational methods for analysis of complex mixtures for application in metabolomics. Our research involves the design of new experimental NMR measurements, high-performance computing for NMR data analysis and structure calculation, and applications to globally interesting biological systems.

Our main objectives aim at an increasingly predictive understanding of globular protein structures and complex protein assemblies, their properties, interactions and function and – as expert in this field – to develop state-of-the-art computational protocols for biomolecular NMR structure determination, notably exploring advanced bioinformatic approaches for big data-mining in order to enable accurate atomic-resolution molecular modeling even in the presence of sparse experimental data.

Biography

Dr. Torsten Herrmann studied Theoretical Physics and Mathematics at the University of Kaiserslautern (Germany), the ETH Zürich (Switzerland) and the Paul Scherrer Institute (Switzerland), where he graduated in 1997. He received his Ph.D. in Natural Sciences at the ETH Zürich with Prof. Kurt Wüthrich in 2002 (Nobel Laureate in Chemistry 2002). After three years as Postdoctoral Fellow at The Scripps Research Institute (San Diego, USA), he returned as Senior Researcher (Oberassistent) to the ETH Zürich in 2005. In Jan. 2008, Dr. Torsten Herrmann got recruited as Group Leader for Structural Biology at the newly founded European Centre for High-Field NMR (CRMN), a research unit of the Ecole Normale Superieure de Lyon (France), and he received the qualification for professorship in Theoretical, Physical and Analytical chemistry by the French Ministry of National Education. In Oct. 2010, Dr. Torsten Herrmann was promoted to CNRS Research Director (Full professor) at the CRMN in Lyon. In Jan. 2014, Dr. Torsten Herrmann was appointed as Group Leader for Computational Methods for Biomolecular Studies at the newly founded Institute for Analytical Sciences (ISA), a joined research institute of the Ecole Normale Superieure de Lyon (ENS Lyon), the Centre National de la Recherche Scientifique (CNRS), and the Universite de Claude Bernard Lyon 1 (UCBL). Concerning institutional appointments, Dr. Torsten Herrmann was elected member of the Unit Council (2013-2016) and Scientific Council member at ISA (2014-present). Dr. Torsten Herrmann served as Scientific Coordinator and Member of the Direction Committee at ISA (2015). Dr. Torsten Herrmann served as Theme Coordinator for Computational Sciences at ISA (2014-2016).

Dr. Torsten Herrmann’s track record comprises more than 60 publications in international peer-reviewed journals, and more than 50 invited talks at international conferences and workshops (H-Index = 31, #citations > 4200). He is co-author of more than 50 NMR structures deposited in the Protein Data Bank (PDB), and he is the author of the UNIO software suite that is more than 1000 times licensed world-wide to academy and industry alike. Dr. Torsten Herrmann is member of several international expert commission: he is founding member of the NMR community-wide stringent blind protein target CASD-NMR initiative for “Critical assessment of automated structure determination of proteins from NMR data” (2009-present), he is nominated member of the NMR task force for structure validation of the world-wide Protein Data Bank (wwPDB) (2009-present), and he is nominated member of the NMR task force for developing a New Exchange Format (NEF) for the wwPDB (2014-present).

Keywords

Nuclear Magnetic Resonance Spectroscopy, Protein NMR, Computational Structural Biology, UNIO, Protein Structure and Dynamics, Proteins, Nucleic Acids, High Performance Scientific Programming

Publications

Publications HAL de torsten,herrmann

2016

Journal articles

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Loren B Andreas, Kristaps Jaudzems, Jan Stanek, Daniela Lalli, Andrea Bertarello, et al.. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR. Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2016, 113 (33), pp.9187-9192. <10.1073/pnas.1602248113>. <hal-01359815>
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Augustyniak Rafal, Stanek Jan, Colaux Henri, Bodenhausen Geoffrey, Koźmiński Wiktor, et al.. Nuclear overhauser spectroscopy of chiral CHD methylene groups. Journal of Biomolecular NMR, Springer Verlag, 2016, 64 (1), pp.27-37. <10.​1007/​s10858-015-0002-0>. <hal-01237902>
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Rafal Augustyniak, Jan Stanek, Henri Colaux, Geoffrey Bodenhausen, Wiktor Kozminski, et al.. Nuclear overhauser spectroscopy of chiral CHD methylene groups. Journal of Biomolecular NMR, Springer Verlag, 2016, 64 (1), pp.27-37. <10.1007/s10858-015-0002-0>. <hal-01366188>
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2015

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Paul Guerry, Viet Dung Duong, Torsten Herrmann. CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO. Journal of Biomolecular NMR, Springer Verlag, 2015, 62 (4), pp.473-480. <10.1007/s10858-015-9934-7>. <hal-01158688>
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Cristiane Latge, Katia M. S. Cabral, Guilherme A. P. De Oliveira, Diana P. Raymundo, Julia A. Freitas, et al.. The solution structure and dynamics of full-length human cerebral dopamine neurotrophic factor and its neuroprotective role against α-synuclein oligomers. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (33), pp.20527-20540. <10.1074/jbc.M115.662254>. <hal-01187615>
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Loren B Andreas, Jan Stanek, Tanguy Le Marchand, Andrea Bertarello, Diane Cala – de Paepe, et al.. Protein residue linking in a single spectrum for magic-angle spinning NMR assignment. Journal of Biomolecular NMR, Springer Verlag, 2015, 62 (3), pp.253-261. <10.1007/s10858-015-9956-1>. <hal-01186756>
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Samit Kumar Dutta, Pedro Serrano, Andrew Proudfoot, Michael Geralt, Bill Pedrini, et al.. APSY-NMR for protein backbone assignment in high-throughput structural biology. Journal of Biomolecular NMR, Springer Verlag, 2015, 61 (1), pp.47-53. <10.1007/s10858-014-9881-8>. <hal-01119529>
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Aleksandras Gutmanas, Paul D Adams, Benjamin Bardiaux, Helen M. Berman, David Case, et al.. NMR Exchange Format: a unified and open standard for representation of NMR restraint data. Nature Structural and Molecular Biology, Nature Publishing Group, 2015, 22, pp.433-434. <10.1038/nsmb.3041>. <hal-01187684>
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2014

Journal articles

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Emeline Barbet-Massin, Andrew J. Pell, Joren S. Retel, Loren B Andreas, Kristaps Jaudzems, et al.. Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning. Journal of the American Chemical Society, American Chemical Society, 2014, 136 (35), pp.12489-12497. <10.1021/ja507382j>. <hal-01070782>
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2013

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T. Montelione Gaetano, Michael Nilges, Ad Bax, Peter Güntert, Torsten Herrmann, et al.. Recommendations of the wwPDB NMR validation task force. Structure, Elsevier (Cell Press), 2013, 21 (9), pp.1563-1570. <10.1016/j.str.2013.07.021>. <hal-00955839>
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2012

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Tsjerk A. Wassenaar, Marc Van Dijk, Nuno Loureiro-Ferreira, Gijs Van Der Schot, Sjoerd J. De Vries, et al.. WeNMR: Structural biology on the grid. Journal of Grid Computing, Springer Verlag, 2012, 10 (4), pp.743-767. <hal-00955902>
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Xiaoxue Wang, Dana M Lord, Hsin-Yao Cheng, Devon O Osbourne, Seok Hoon Hong, et al.. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS.. Nature Chemical Biology, Nature Publishing Group, 2012, 8 (10), pp.855-861. <10.1038/nchembio.1062>. <hal-00955874>
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Michael J. Knight, Isabella C. Felli, Roberta Pierattelli, Ivano Bertini, Lyndon Emsley, et al.. Rapid Measurement of Pseudocontact Shifts in Metalloproteins by Proton-Detected Solid-State NMR Spectroscopy. Journal of the American Chemical Society, American Chemical Society, 2012, 134 (36), pp.14730-14733. <10.1021/ja306813j>. <hal-00799577>
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Pedro Serrano, Bill Pedrini, Biswaranjan Mohanty, Michael Geralt, Torsten Herrmann, et al.. The J-UNIO protocol for automated protein structure determination by NMR in solution. Journal of Biomolecular NMR, Springer Verlag, 2012, 53 (4), pp.341-354. <10.1007/s10858-012-9645-2>. <hal-00799605>
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Antonio Rosato, James Aramini, Cheryl Arrowsmith, Anurag Bagaria, David Baker, et al.. Blind Testing of Routine, Fully Automated Determination of Protein Structures from NMR Data. Structure, Elsevier (Cell Press), 2012, 20 (2), pp.227-236. <10.1016/j.str.2012.01.002>. <hal-00698571>
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Michael J. Knight, Andrew J. Pell, Ivano Bertini, Isabella C. Felli, Leonardo Gonnelli, et al.. Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2012, 109 (28), pp.11095-11100. <10.1073/pnas.1204515109>. <hal-00809200>
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2011

Journal articles

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Paul Guerry, Torsten Herrmann. Advances in automated NMR protein structure determination.. Quarterly Reviews of Biophysics, Cambridge University Press (CUP), 2011, 44 (3), pp.257-309. <10.1017/S0033583510000326>. <hal-00700390>
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Dijk Van, Schot Van Der, Vries De, Zwan Van Der, T.A. Wassenaar, et al.. WeNMR: Structural Biology on the Grid. IWSG-Life, 2011. <hal-01238421>
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Daniel Burschowsky, Fabian Rudolf, Gwénaël Rabut, Torsten Herrmann, Matthias Peter, et al.. Structural analysis of the conserved ubiquitin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (2), pp.1364-73. <10.1074/jbc.M110.135038>. <inserm-00629426>
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Michael J. Knight, Amy L. Webber, Andrew J. Pell, Paul Guerry, Emeline Barbet-Massin, et al.. Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid-state MAS NMR spectroscopy. Angewandte Chemie International Edition, Wiley-VCH Verlag, 2011, 50 (49), pp.11697-11701. <10.1002/anie.201106340>. <hal-00809132>
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