Eidgenössische Technische Hochschule Zurich (ETHZ), Switzerland, 1970-74: Diploma in chemistry. University of Oxford, England, 1975-77: Doctoral thesis (D.Phil.), Prof. Ray Freeman, FRS. University of California at San Diego, La Jolla, 1978: post-doctoral fellow, Prof. Robert Vold and Prof. Regitze Vold. Massachusetts Institute of Technology (MIT), Francis Bitter National Magnet Laboratory, 1979-80: Research associate, Dr Leo Neuringer and prof Robert Griffin. ETHZ, 1980-85: Teaching assistant and Privatdozent, prof Richard Ernst. Institute of Organic Chemistry, University of Lausanne, 1985-94: Associate Professor. Department of Chemistry, Florida State University, Tallahassee, 1994-1996: Professor. National High Magnetic Field Laboratory, Tallahassee, 1994 -1996: Director of Nuclear Magnetic Resonance Program. Swiss Federal Institute of Technology (EPFL), Lausanne, 2016-present: Honorary Professor. Department of Chemistry, Ecole Normale Supérieure, Paris, 2019-present: Professor emeritus. Scholarship of the Salter’s Company, London (1976). National Latsis Prize awarded by the Swiss National Science Foundation (1990). Doctor honoris causa, University of Stockholm (1993). Fellow, American Physical Society (1996). Corresponding member, Royal Academy of Sciences of the Netherlands (1997). Catalan-Sabatier Prize, Royal Society of Chemistry of Spain (2006). Fellow, International Society of Magnetic Resonance (ISMAR) (2008). Chevalier de la Légion d’honneur (2017). Günther Laukien prize (2019). Chair, Board of Trustees, European Magnetic Resonance Conferences (EUROMAR) (2005-2011). Chair, Symposium on Dynamic Nuclear Polarization, Lausanne, 2011. Chair, Alpine Conference on Solid-State NMR, Chamonix, 2011. Member of the Editorial Board, "Journal of Magnetic Resonance", San Diego, since 1996. Member of the Editorial Board, "Progress in NMR Spectroscopy”, since 2012. Chair, Editorial Board, "Magnetic Resonance”, since 2019.

Eidgenössische Technische Hochschule Zurich (ETHZ), Switzerland, 1970-74: Diploma in chemistry. University of Oxford, England, 1975-77: Doctoral thesis (D.Phil.), Prof. Ray Freeman, FRS. University of California at San Diego, La Jolla, 1978: post-doctoral fellow, Prof. Robert Vold and Prof. Regitze Vold. Massachusetts Institute of Technology (MIT), Francis Bitter National Magnet Laboratory, 1979-80: Research associate, Dr Leo Neuringer and prof Robert Griffin. ETHZ, 1980-85: Teaching assistant and Privatdozent, prof Richard Ernst. Institute of Organic Chemistry, University of Lausanne, 1985-94: Associate Professor. Department of Chemistry, Florida State University, Tallahassee, 1994-1996: Professor. National High Magnetic Field Laboratory, Tallahassee, 1994 -1996: Director of Nuclear Magnetic Resonance Program. Swiss Federal Institute of Technology (EPFL), Lausanne, 2016-present: Honorary Professor. Department of Chemistry, Ecole Normale Supérieure, Paris, 2019-present: Professor emeritus. Scholarship of the Salter’s Company, London (1976). National Latsis Prize awarded by the Swiss National Science Foundation (1990). Doctor honoris causa, University of Stockholm (1993). Fellow, American Physical Society (1996). Corresponding member, Royal Academy of Sciences of the Netherlands (1997). Catalan-Sabatier Prize, Royal Society of Chemistry of Spain (2006). Fellow, International Society of Magnetic Resonance (ISMAR) (2008). Chevalier de la Légion d’honneur (2017). Günther Laukien prize (2019). Chair, Board of Trustees, European Magnetic Resonance Conferences (EUROMAR) (2005-2011). Chair, Symposium on Dynamic Nuclear Polarization, Lausanne, 2011. Chair, Alpine Conference on Solid-State NMR, Chamonix, 2011. Member of the Editorial Board, "Journal of Magnetic Resonance", San Diego, since 1996. Member of the Editorial Board, "Progress in NMR Spectroscopy”, since 2012. Chair, Editorial Board, "Magnetic Resonance”, since 2019.

After a PhD at ETH Zurich with Richard Ernst in liquid-state NMR (cross-correlated cross relaxation), I moved to UC Berkeley for a postdoc with Alexander Pines where I started to work on solid-state NMR. Since then, I have been interested in and working on method development in high-resolution NMR under magic-angle spinning. My interests also include numerical simulations of spin systems and the theory of NMR under MAS and how to characterize Hamiltonians with multiple time depencies. In addition, my group also works on dissolution DNP methodology and hardware development in this area. Currently, I am an adjunct professor at Physical Chemistry, ETH Zürich, Switzerland.

After a PhD at ETH Zurich with Richard Ernst in liquid-state NMR (cross-correlated cross relaxation), I moved to UC Berkeley for a postdoc with Alexander Pines where I started to work on solid-state NMR. Since then, I have been interested in and working on method development in high-resolution NMR under magic-angle spinning. My interests also include numerical simulations of spin systems and the theory of NMR under MAS and how to characterize Hamiltonians with multiple time depencies. In addition, my group also works on dissolution DNP methodology and hardware development in this area. Currently, I am an adjunct professor at Physical Chemistry, ETH Zürich, Switzerland.

+41 44 6324366

+61-2-61256507

As a graduate student at Yale, I helped develop residual dipolar coupling methodology for studying the structure and dynamics of proteins by NMR. Applying these methods to nucleic acids as a postdoctoral fellow at the Memorial Sloan Kettering Cancer Center, I began to probe the dynamics of RNA and DNA at atomic resolution. As an independent PI, my group developed NMR methods for visualizing the structural dynamics of DNA and RNA at atomic resolution and over timescales spanning twelve orders of magnitude from picoseconds to seconds. Now at Duke University, my group continues to develop NMR based techniques to push structural biology from static 3D snapshots toward 4D ‘movies’ of biomolecules in functional motion. Our research group has characterized many motional modes that underlie the biological activities of nucleic acids, with important implications for drug discovery and for understanding the mechanisms of non-coding RNAs and the processes that cause genome instability and cancer. These motions include transitions between Watson-Crick and Hoogsteen base pairs which shape the DNA protein recognition and damage landscapea; transitions between mismatch and tautomeric/anionic Watson-Crick base pairs, which are responsible for errors during replication, transcription, and translationb; motions that determine proper folding of RNAc; and transient changes in RNA secondary structure that underlie gene regulation and viral genomic replication by non-coding RNAsd. My group has also developed methods for targeting RNA with small molecules based on RNA structural dynamics. The ultimate goal of my academic research program is to obtain a deep and predictive understanding regarding the cellular activity of nucleic acids in vivo, and to apply this knowledge in drug discovery and synthetic biology.

As a graduate student at Yale, I helped develop residual dipolar coupling methodology for studying the structure and dynamics of proteins by NMR. Applying these methods to nucleic acids as a postdoctoral fellow at the Memorial Sloan Kettering Cancer Center, I began to probe the dynamics of RNA and DNA at atomic resolution. As an independent PI, my group developed NMR methods for visualizing the structural dynamics of DNA and RNA at atomic resolution and over timescales spanning twelve orders of magnitude from picoseconds to seconds. Now at Duke University, my group continues to develop NMR based techniques to push structural biology from static 3D snapshots toward 4D ‘movies’ of biomolecules in functional motion. Our research group has characterized many motional modes that underlie the biological activities of nucleic acids, with important implications for drug discovery and for understanding the mechanisms of non-coding RNAs and the processes that cause genome instability and cancer. These motions include transitions between Watson-Crick and Hoogsteen base pairs which shape the DNA protein recognition and damage landscapea; transitions between mismatch and tautomeric/anionic Watson-Crick base pairs, which are responsible for errors during replication, transcription, and translationb; motions that determine proper folding of RNAc; and transient changes in RNA secondary structure that underlie gene regulation and viral genomic replication by non-coding RNAsd. My group has also developed methods for targeting RNA with small molecules based on RNA structural dynamics. The ultimate goal of my academic research program is to obtain a deep and predictive understanding regarding the cellular activity of nucleic acids in vivo, and to apply this knowledge in drug discovery and synthetic biology.

+33617126833

Prof Barth’s main interests are in the fields of MR method development for applications in neuroimaging with a focus on functional MRI and neurological diseases such as dementia and cancer, as well as cardiac MR.

Prof Barth’s main interests are in the fields of MR method development for applications in neuroimaging with a focus on functional MRI and neurological diseases such as dementia and cancer, as well as cardiac MR.

+49-30-838-56049

My reserach interest is in structural biology, and more precisely protein solid-state NMR. After a PhD in solution NMR, I learned this new technique during my post-doc in New York. In Lyon, I first worked on establishing NMR techniques using model molecules, and developed sequential assignment and distance measurements, the two building blocks enabling to investigate protein structures by NMR. I then turned to structural studies of fibrillar proteins, including the yeast prions Ure2p and Sup35, as well as the amyloids A-β and α-synuclein, involved in Alzheimer and Parkinson’s diseases, and also amyloid fibrils involved in light chain disease. More recently, my lab turns to the investigation of membrane proteins, including model systems like the ABC transporter BmrA, and the studies large protein assemblies, notably of viral (membrane) proteins from hepatitis B/C and Dengue virus.

My reserach interest is in structural biology, and more precisely protein solid-state NMR. After a PhD in solution NMR, I learned this new technique during my post-doc in New York. In Lyon, I first worked on establishing NMR techniques using model molecules, and developed sequential assignment and distance measurements, the two building blocks enabling to investigate protein structures by NMR. I then turned to structural studies of fibrillar proteins, including the yeast prions Ure2p and Sup35, as well as the amyloids A-β and α-synuclein, involved in Alzheimer and Parkinson’s diseases, and also amyloid fibrils involved in light chain disease. More recently, my lab turns to the investigation of membrane proteins, including model systems like the ABC transporter BmrA, and the studies large protein assemblies, notably of viral (membrane) proteins from hepatitis B/C and Dengue virus.

Eidgenössische Technische Hochschule Zurich (ETHZ), Switzerland, 1970-74: Diploma in chemistry. University of Oxford, England, 1975-77: Doctoral thesis (D.Phil.), Prof. Ray Freeman, FRS. University of California at San Diego, La Jolla, 1978: post-doctoral fellow, Prof. Robert Vold and Prof. Regitze Vold. Massachusetts Institute of Technology (MIT), Francis Bitter National Magnet Laboratory, 1979-80: Research associate, Dr Leo Neuringer and prof Robert Griffin. ETHZ, 1980-85: Teaching assistant and Privatdozent, prof Richard Ernst. Institute of Organic Chemistry, University of Lausanne, 1985-94: Associate Professor. Department of Chemistry, Florida State University, Tallahassee, 1994-1996: Professor. National High Magnetic Field Laboratory, Tallahassee, 1994 -1996: Director of Nuclear Magnetic Resonance Program. Swiss Federal Institute of Technology (EPFL), Lausanne, 2016-present: Honorary Professor. Department of Chemistry, Ecole Normale Supérieure, Paris, 2019-present: Professor emeritus. Scholarship of the Salter’s Company, London (1976). National Latsis Prize awarded by the Swiss National Science Foundation (1990). Doctor honoris causa, University of Stockholm (1993). Fellow, American Physical Society (1996). Corresponding member, Royal Academy of Sciences of the Netherlands (1997). Catalan-Sabatier Prize, Royal Society of Chemistry of Spain (2006). Fellow, International Society of Magnetic Resonance (ISMAR) (2008). Chevalier de la Légion d’honneur (2017). Günther Laukien prize (2019). Chair, Board of Trustees, European Magnetic Resonance Conferences (EUROMAR) (2005-2011). Chair, Symposium on Dynamic Nuclear Polarization, Lausanne, 2011. Chair, Alpine Conference on Solid-State NMR, Chamonix, 2011. Member of the Editorial Board, "Journal of Magnetic Resonance", San Diego, since 1996. Member of the Editorial Board, "Progress in NMR Spectroscopy”, since 2012. Chair, Editorial Board, "Magnetic Resonance”, since 2019.

Eidgenössische Technische Hochschule Zurich (ETHZ), Switzerland, 1970-74: Diploma in chemistry. University of Oxford, England, 1975-77: Doctoral thesis (D.Phil.), Prof. Ray Freeman, FRS. University of California at San Diego, La Jolla, 1978: post-doctoral fellow, Prof. Robert Vold and Prof. Regitze Vold. Massachusetts Institute of Technology (MIT), Francis Bitter National Magnet Laboratory, 1979-80: Research associate, Dr Leo Neuringer and prof Robert Griffin. ETHZ, 1980-85: Teaching assistant and Privatdozent, prof Richard Ernst. Institute of Organic Chemistry, University of Lausanne, 1985-94: Associate Professor. Department of Chemistry, Florida State University, Tallahassee, 1994-1996: Professor. National High Magnetic Field Laboratory, Tallahassee, 1994 -1996: Director of Nuclear Magnetic Resonance Program. Swiss Federal Institute of Technology (EPFL), Lausanne, 2016-present: Honorary Professor. Department of Chemistry, Ecole Normale Supérieure, Paris, 2019-present: Professor emeritus. Scholarship of the Salter’s Company, London (1976). National Latsis Prize awarded by the Swiss National Science Foundation (1990). Doctor honoris causa, University of Stockholm (1993). Fellow, American Physical Society (1996). Corresponding member, Royal Academy of Sciences of the Netherlands (1997). Catalan-Sabatier Prize, Royal Society of Chemistry of Spain (2006). Fellow, International Society of Magnetic Resonance (ISMAR) (2008). Chevalier de la Légion d’honneur (2017). Günther Laukien prize (2019). Chair, Board of Trustees, European Magnetic Resonance Conferences (EUROMAR) (2005-2011). Chair, Symposium on Dynamic Nuclear Polarization, Lausanne, 2011. Chair, Alpine Conference on Solid-State NMR, Chamonix, 2011. Member of the Editorial Board, "Journal of Magnetic Resonance", San Diego, since 1996. Member of the Editorial Board, "Progress in NMR Spectroscopy”, since 2012. Chair, Editorial Board, "Magnetic Resonance”, since 2019.

Bernhard Brutscher received a B.S. in Physics from the University of Karlsruhe in 1992, and a Ph.D. from the University Grenoble in 1995. From 1996-1997, he stayed as a postdoc at ETH Zürich in the NMR group of Prof. R.R. Ernst. Since 1997 he is a staff scientist at the Institute of Structural Biology (IBS) in Grenoble. His major research interests are methodological developments for NMR studies of structure and dynamics of proteins and nucleic acids.

Bernhard Brutscher received a B.S. in Physics from the University of Karlsruhe in 1992, and a Ph.D. from the University Grenoble in 1995. From 1996-1997, he stayed as a postdoc at ETH Zürich in the NMR group of Prof. R.R. Ernst. Since 1997 he is a staff scientist at the Institute of Structural Biology (IBS) in Grenoble. His major research interests are methodological developments for NMR studies of structure and dynamics of proteins and nucleic acids.

The main focus of Robin de Graaf's research is the development of in vivo MR methods and hardware to study cerebral energy metabolism in human and animal brains. NMR spectroscopy (proton, (inverse) carbon-13, deuterium and phosphorus-31) is the most important tool in the study of metabolic processes and fluxes, non-invasively in vivo. Besides studying brain energy metabolism, a significant part of the research is reserved for technological and methodological improvements to the technique of NMR spectroscopy. These include methods for better water and lipid suppression, spatial localization, spectral editing, quantification, and shimming. Robin's current research focus covers areas that are all related to tackling the challenges and grasping the opportunities of MR at high magnetic fields.

The main focus of Robin de Graaf's research is the development of in vivo MR methods and hardware to study cerebral energy metabolism in human and animal brains. NMR spectroscopy (proton, (inverse) carbon-13, deuterium and phosphorus-31) is the most important tool in the study of metabolic processes and fluxes, non-invasively in vivo. Besides studying brain energy metabolism, a significant part of the research is reserved for technological and methodological improvements to the technique of NMR spectroscopy. These include methods for better water and lipid suppression, spatial localization, spectral editing, quantification, and shimming. Robin's current research focus covers areas that are all related to tackling the challenges and grasping the opportunities of MR at high magnetic fields.

I am a CNRS associate scientist at the CEISAM research institute in Nantes. I work on the development of NMR methods, mainly for the analysis of small-molecules mixtures.

I am a CNRS associate scientist at the CEISAM research institute in Nantes. I work on the development of NMR methods, mainly for the analysis of small-molecules mixtures.

+33 2 51 12 57 01‬

After a PhD at ETH Zurich with Richard Ernst in liquid-state NMR (cross-correlated cross relaxation), I moved to UC Berkeley for a postdoc with Alexander Pines where I started to work on solid-state NMR. Since then, I have been interested in and working on method development in high-resolution NMR under magic-angle spinning. My interests also include numerical simulations of spin systems and the theory of NMR under MAS and how to characterize Hamiltonians with multiple time depencies. In addition, my group also works on dissolution DNP methodology and hardware development in this area. Currently, I am an adjunct professor at Physical Chemistry, ETH Zürich, Switzerland.

After a PhD at ETH Zurich with Richard Ernst in liquid-state NMR (cross-correlated cross relaxation), I moved to UC Berkeley for a postdoc with Alexander Pines where I started to work on solid-state NMR. Since then, I have been interested in and working on method development in high-resolution NMR under magic-angle spinning. My interests also include numerical simulations of spin systems and the theory of NMR under MAS and how to characterize Hamiltonians with multiple time depencies. In addition, my group also works on dissolution DNP methodology and hardware development in this area. Currently, I am an adjunct professor at Physical Chemistry, ETH Zürich, Switzerland.

+41 44 6324366

Patrick Giraudeau is a Professor at the University of Nantes. He specializes on the development of liquid-state NMR methods for the accurate quantitative analysis of complex mixtures, for applications such as metabolomics or reaction monitoring. His current research interests include fast quantitative multi-dimensional methods, dissolution-DNP (dynamic nuclear polarization), and more generally fast quantitative pulse sequences at high-field as well as for benchtop spectrometers. Patrick Giraudeau graduated from the University of Nantes (PhD 2009, Habilitation 2012), and did a post-doc at the Weizmann Institute of Science (Israel). He is an honorary member of the Institut Universitaire de France and was awarded an ERC Consolidator Grant in 2018. He is the vice-president of the French-speaking Metabolomics and Fluxomics Network (RFMF) since 2015. Finally, Patrick Giraudeau is a committee member of the Groupement Ampere and a member of the Euromar Board of Trustees.

Patrick Giraudeau is a Professor at the University of Nantes. He specializes on the development of liquid-state NMR methods for the accurate quantitative analysis of complex mixtures, for applications such as metabolomics or reaction monitoring. His current research interests include fast quantitative multi-dimensional methods, dissolution-DNP (dynamic nuclear polarization), and more generally fast quantitative pulse sequences at high-field as well as for benchtop spectrometers. Patrick Giraudeau graduated from the University of Nantes (PhD 2009, Habilitation 2012), and did a post-doc at the Weizmann Institute of Science (Israel). He is an honorary member of the Institut Universitaire de France and was awarded an ERC Consolidator Grant in 2018. He is the vice-president of the French-speaking Metabolomics and Fluxomics Network (RFMF) since 2015. Finally, Patrick Giraudeau is a committee member of the Groupement Ampere and a member of the Euromar Board of Trustees.

My research focuses on the development and application of multidimensional and multinuclear solid-state NMR techniques to elucidate the structure and dynamics of membrane proteins and other biological macromolecules. In the area of membrane proteins, we are particularly interested in the biophysical chemistry and mechanisms of action of ion channels and curvature-inducing membrane proteins such as viral fusion proteins and antimicrobial peptides. Our research has elucidated the proton-conduction mechanism and drug-inhibition mechanism of influenza M2 proteins, the oligomeric structure and membrane-disruptive mechanism of β-hairpin antimicrobial peptides, and the conformation and dynamics of channel-forming colicin Ia for its spontaneous insertion into the lipid membrane. We also investigate the structure and dynamics of complex polysaccharides such as cellulose, hemicellulose, and pectins in plant cell walls and amyloid fibrils involved in neurodegenerative diseases. To answer these biophysical questions, we develop a wide range of solid-state NMR techniques such as novel isotopic labeling strategies, multidimensional correlation techniques, polarization transfer pulse sequences, and computational methods. These new techniques allow efficient assignment of protein NMR spectra, increase the distance range of NMR from angstroms to nanometers, probe the insertion depth of membrane proteins, measure protein orientation in phospholipid bilayers, and detect intermolecular binding such as protein-drug, protein-cholesterol and protein-polysaccharide binding. These methods have allowed us to obtain detailed mechanistic insights about proteins and carbohydrates that cannot be obtained from any other high-resolution structural techniques.

My research focuses on the development and application of multidimensional and multinuclear solid-state NMR techniques to elucidate the structure and dynamics of membrane proteins and other biological macromolecules. In the area of membrane proteins, we are particularly interested in the biophysical chemistry and mechanisms of action of ion channels and curvature-inducing membrane proteins such as viral fusion proteins and antimicrobial peptides. Our research has elucidated the proton-conduction mechanism and drug-inhibition mechanism of influenza M2 proteins, the oligomeric structure and membrane-disruptive mechanism of β-hairpin antimicrobial peptides, and the conformation and dynamics of channel-forming colicin Ia for its spontaneous insertion into the lipid membrane. We also investigate the structure and dynamics of complex polysaccharides such as cellulose, hemicellulose, and pectins in plant cell walls and amyloid fibrils involved in neurodegenerative diseases. To answer these biophysical questions, we develop a wide range of solid-state NMR techniques such as novel isotopic labeling strategies, multidimensional correlation techniques, polarization transfer pulse sequences, and computational methods. These new techniques allow efficient assignment of protein NMR spectra, increase the distance range of NMR from angstroms to nanometers, probe the insertion depth of membrane proteins, measure protein orientation in phospholipid bilayers, and detect intermolecular binding such as protein-drug, protein-cholesterol and protein-polysaccharide binding. These methods have allowed us to obtain detailed mechanistic insights about proteins and carbohydrates that cannot be obtained from any other high-resolution structural techniques.

I am active in NMR methods development and applications, in particular through on NMR of quadrupolar nuclei and the miniaturization of NMR detectors for solid- and liquid-state NMR. The introduction of the rotor-synchronized 2D-exchange experiment and the development of adiabatic excitation methods have found widespread application. In solid-state NMR we introduced the concept of microcoils for powdered samples. For flat geometries we introduced the stripline resonator giving unsurpassed sensitivity and resolution in microfluidic applications and thin film analyses. Finally, we introduced the so-called piggy-back Magic Angle Spinning approach, proving that high-resolution solid-state NMR of nanoliter quantities of materials is feasible and viable. The technique developments described above are not a goal on their own, it is strived to apply the methods in relevant materials research. The emphasis is on materials for energy storage and conversion and catalysts. Linking chemically specific structure information to physical properties of polymers is a further important activity in this area. Finally, in liquid-state NMR we focus on the analysis of complex mixtures in a microfluidic context.

I am active in NMR methods development and applications, in particular through on NMR of quadrupolar nuclei and the miniaturization of NMR detectors for solid- and liquid-state NMR. The introduction of the rotor-synchronized 2D-exchange experiment and the development of adiabatic excitation methods have found widespread application. In solid-state NMR we introduced the concept of microcoils for powdered samples. For flat geometries we introduced the stripline resonator giving unsurpassed sensitivity and resolution in microfluidic applications and thin film analyses. Finally, we introduced the so-called piggy-back Magic Angle Spinning approach, proving that high-resolution solid-state NMR of nanoliter quantities of materials is feasible and viable. The technique developments described above are not a goal on their own, it is strived to apply the methods in relevant materials research. The emphasis is on materials for energy storage and conversion and catalysts. Linking chemically specific structure information to physical properties of polymers is a further important activity in this area. Finally, in liquid-state NMR we focus on the analysis of complex mixtures in a microfluidic context.

Educated at Latvian University, Riga; PhD and Dr. Hab. from Latvian Institute of Organic Synthesis, Riga; AvHumboldt Fellowship with Prof. B. Wrackmeyer Bayreuth, Germany; Postdoc with Prof. Ray Freeman, Cambridge, UK and Iain Campbell, Oxford, UK; Joined Varian Associates in 1995 and Visiting Scientist with Prof. G. Wagner, Harvard Medical School, 1995-1996; Principal Scientist with Bruker BioSpin 2013-2023. Varian Fellow since 2008 and Agilent Research Fellow since 2011. Elected member of Latvian Academy of Sciences since 2011.

Educated at Latvian University, Riga; PhD and Dr. Hab. from Latvian Institute of Organic Synthesis, Riga; AvHumboldt Fellowship with Prof. B. Wrackmeyer Bayreuth, Germany; Postdoc with Prof. Ray Freeman, Cambridge, UK and Iain Campbell, Oxford, UK; Joined Varian Associates in 1995 and Visiting Scientist with Prof. G. Wagner, Harvard Medical School, 1995-1996; Principal Scientist with Bruker BioSpin 2013-2023. Varian Fellow since 2008 and Agilent Research Fellow since 2011. Elected member of Latvian Academy of Sciences since 2011.

Malcolm H Levitt: born 1957, Hull, England. Undergraduate education: Keble College, Oxford 1973–1978. BA Chem (Oxon) in 1978, D Phil with Ray Freeman, Oxford, 1981. Postdoctoral research with Shimon Vega (Weizmann Institute, Israel) 1982 and R. R. Ernst (ETH-Zürich, 1982–1985). Staff scientist at the Francis Bitter National Magnet Laboratory, MIT, 1985–1990. Royal Society Research Fellow at the University of Cambridge, UK, 1990–1991. Lecturer and later Professor at the University of Stockholm, Sweden, 1991–2001. Since 2001 Professor in Physical Chemistry, School of Chemistry, Southampton University, UK. Principal honours: LATSIS Research Prize of ETH-Zürich, 1985. Göran Gustafsson Prize in Chemistry, Sweden, 1996. Ampère Prize of the International Society of Magnetic Resonance, 2005. Honorary Fellow of the Indian Society of Magnetic Resonance, 2006. Adjunct Professorship of the Tata Institute of Fundamental Research, Mumbai, India, 2006. Fellow of the Royal Society, 2007. Laukien Prize in Magnetic Resonance, 2008. Fellow of the International Society of Magnetic Resonance, 2008. Craig Lectureship, Australian National University, 2010. Fellow of the National Academy of Sciences, India, 2012. Russell Varian Prize in Nuclear Magnetic Resonance, 2015.

Malcolm H Levitt: born 1957, Hull, England. Undergraduate education: Keble College, Oxford 1973–1978. BA Chem (Oxon) in 1978, D Phil with Ray Freeman, Oxford, 1981. Postdoctoral research with Shimon Vega (Weizmann Institute, Israel) 1982 and R. R. Ernst (ETH-Zürich, 1982–1985). Staff scientist at the Francis Bitter National Magnet Laboratory, MIT, 1985–1990. Royal Society Research Fellow at the University of Cambridge, UK, 1990–1991. Lecturer and later Professor at the University of Stockholm, Sweden, 1991–2001. Since 2001 Professor in Physical Chemistry, School of Chemistry, Southampton University, UK. Principal honours: LATSIS Research Prize of ETH-Zürich, 1985. Göran Gustafsson Prize in Chemistry, Sweden, 1996. Ampère Prize of the International Society of Magnetic Resonance, 2005. Honorary Fellow of the Indian Society of Magnetic Resonance, 2006. Adjunct Professorship of the Tata Institute of Fundamental Research, Mumbai, India, 2006. Fellow of the Royal Society, 2007. Laukien Prize in Magnetic Resonance, 2008. Fellow of the International Society of Magnetic Resonance, 2008. Craig Lectureship, Australian National University, 2010. Fellow of the National Academy of Sciences, India, 2012. Russell Varian Prize in Nuclear Magnetic Resonance, 2015.

NMR, solid-state NMR in particular. Methods development and applications in biophysics and materials science.

NMR, solid-state NMR in particular. Methods development and applications in biophysics and materials science.

+61-2-61256507

Jeffrey A. Reimer received his bachelor’s degree (with honors) from the University of California at Santa Barbara, and his doctorate from the California Institute of Technology. Prior to his faculty appointment at UC Berkeley he was a postdoctoral fellow at IBM Research in Yorktown Heights, New York. He is presently the C. Judson King Endowed Professor and the Warren and Katharine Schlinger Distinguished Professor and Chair of the Chemical and Biomolecular Engineering Department. Professor Reimer has won several teaching awards, including the UC Berkeley Distinguished Teaching Award, the highest award bestowed on faculty for their teaching. Professor Reimer’s scholarship is in the fields of materials chemistry and engineering, with particular attention to the application of sophisticated NMR spectroscopic and physical measurements. He is recognized for these works by election as a Fellow of the American Association for the Advancement of Science, a Fellow of the American Physical Society in the Division of Materials Physics, and a Fellow of the International Society for Magnetic Resonance. In 2015 Professor Reimer was the recipient of a Research Fellowship from the Alexander von Humboldt Foundation. In addition to his ~210 research publications, Professor Reimer is co-author (with T.M. Duncan) of the introductory text Chemical Engineering Design and Analysis (Cambridge University Press, 2nd Edition, 2019), and the text Carbon Capture and Sequestration (with Berend Smit, Curt Oldenburg, Ian Bourg, World Scientific Press, 2013).

Jeffrey A. Reimer received his bachelor’s degree (with honors) from the University of California at Santa Barbara, and his doctorate from the California Institute of Technology. Prior to his faculty appointment at UC Berkeley he was a postdoctoral fellow at IBM Research in Yorktown Heights, New York. He is presently the C. Judson King Endowed Professor and the Warren and Katharine Schlinger Distinguished Professor and Chair of the Chemical and Biomolecular Engineering Department. Professor Reimer has won several teaching awards, including the UC Berkeley Distinguished Teaching Award, the highest award bestowed on faculty for their teaching. Professor Reimer’s scholarship is in the fields of materials chemistry and engineering, with particular attention to the application of sophisticated NMR spectroscopic and physical measurements. He is recognized for these works by election as a Fellow of the American Association for the Advancement of Science, a Fellow of the American Physical Society in the Division of Materials Physics, and a Fellow of the International Society for Magnetic Resonance. In 2015 Professor Reimer was the recipient of a Research Fellowship from the Alexander von Humboldt Foundation. In addition to his ~210 research publications, Professor Reimer is co-author (with T.M. Duncan) of the introductory text Chemical Engineering Design and Analysis (Cambridge University Press, 2nd Edition, 2019), and the text Carbon Capture and Sequestration (with Berend Smit, Curt Oldenburg, Ian Bourg, World Scientific Press, 2013).

Kay Saalwächter has studied chemistry at the universities of Mainz and Freiburg, Germany. After his diploma work in Freiburg in the field of light scattering on polymer solutions, he has switched to the field of NMR, working with Klaus Schmidt-Rohr and Hans-Wolfgang Spiess at UMass Amherst (USA) and at the Max-Planck-Institute of Polymer Research in Mainz, respectively. He obtained his doctorate in 2000, and after his habilitation work in Freiburg with Heino Finkelmann in the field of NMR as applied to polymers, he was appointed professor of experimental physics at the Martin-Luther-University Halle-Wittenberg, Germany, in 2005. Research in his group is concerned with the investigation of structure and dynamics in complex "soft" materials, mostly using established and newly developed (solid-state) NMR spectroscopy methods. Under study are the local and chain dynamics, diffusion, as well as molecular and mesoscale structure in polymer melts, dry and swollen elastomers, semicrystalline polymers and block copolymers, liquid crystals and liquid-crystalline polymers. Recent projects include the study of polymer dynamics and ordering in confined geometry (nano-channels and surfaces), biomolecular dynamics and crowding, and interactions of synthetic and biological (macro-)molecules with lipid membranes.

Kay Saalwächter has studied chemistry at the universities of Mainz and Freiburg, Germany. After his diploma work in Freiburg in the field of light scattering on polymer solutions, he has switched to the field of NMR, working with Klaus Schmidt-Rohr and Hans-Wolfgang Spiess at UMass Amherst (USA) and at the Max-Planck-Institute of Polymer Research in Mainz, respectively. He obtained his doctorate in 2000, and after his habilitation work in Freiburg with Heino Finkelmann in the field of NMR as applied to polymers, he was appointed professor of experimental physics at the Martin-Luther-University Halle-Wittenberg, Germany, in 2005. Research in his group is concerned with the investigation of structure and dynamics in complex "soft" materials, mostly using established and newly developed (solid-state) NMR spectroscopy methods. Under study are the local and chain dynamics, diffusion, as well as molecular and mesoscale structure in polymer melts, dry and swollen elastomers, semicrystalline polymers and block copolymers, liquid crystals and liquid-crystalline polymers. Recent projects include the study of polymer dynamics and ordering in confined geometry (nano-channels and surfaces), biomolecular dynamics and crowding, and interactions of synthetic and biological (macro-)molecules with lipid membranes.

+49-345-55-28560

Dr. Michael F. Summers received his A.A. degree from St. Petersburgh Junior College (1978), B.S. from the University of West Florida (1980), Ph.D. from Emory University (1984), and was a postdoctoral fellow at the NIH (1984-1987) before joining the faculty at the University of Maryland Baltimore County as an Assistant Professor in 1987. In 1994 he was appointed as an Investigator with the Howard Hughes Medical Institute, and in 2016 he was elected to the National Academy of Sciences. Dr. Summers’ research focuses on NMR studies of macromolecular structure and interactions, with a major emphasis on the structural proteins and genome of the human immunodeficiency virus (HIV-1). His laboratory typically includes large numbers of students from diverse backgrounds, and he has led efforts to develop programs for retaining minority students in the sciences.

Dr. Michael F. Summers received his A.A. degree from St. Petersburgh Junior College (1978), B.S. from the University of West Florida (1980), Ph.D. from Emory University (1984), and was a postdoctoral fellow at the NIH (1984-1987) before joining the faculty at the University of Maryland Baltimore County as an Assistant Professor in 1987. In 1994 he was appointed as an Investigator with the Howard Hughes Medical Institute, and in 2016 he was elected to the National Academy of Sciences. Dr. Summers’ research focuses on NMR studies of macromolecular structure and interactions, with a major emphasis on the structural proteins and genome of the human immunodeficiency virus (HIV-1). His laboratory typically includes large numbers of students from diverse backgrounds, and he has led efforts to develop programs for retaining minority students in the sciences.

4104552527

For phD study (1979 to 1984), my research interest was in structural organic chemistry, especially, steric strain in overcrowded molecules. I synthesized several model compounds having a methyl group in crowded environment and determined its activation energy for rotation in solids. For determination, I observed 1H spin-lattice relaxation using a so-called wideline NMR spectrometer. After PhD study, I took a Post-Doc position under Prof. C.A. McDowell at British Columbia University (Canada). I studied hydrogen bonding in keto-enol syetems by measuring 13C shielding tensors using a single crystal sample. Further, I developed several new methods (pulse sequences). Some of the sequences (TAPF and TREV) are still frequently used/cited in recent papers. After spending approximately 2.5 years in Canada, I moved to Berkeley to work with Prof. A. Pines as a Post-Doc. At Berkeley, I learned how to start a new thing by doing zero-field NMR and Xenon-NMR. At the end of 1986, I returned to Japan, and started working as a researcher at Foundation of Material Science and Technologies in Tokyo. After working approximately for 0.5 year, I moved to Department of Polymer Science, Faculty of Science, Hokkaido University as an Assistant Professor. After spending 5 years at Hokkaido studying mainly on polymer-blends, I came back to Kyoto University as an Associate Professor to work with Prof. Terao. In Kyoto, I started to develop solid-state NMR methods for determination of structure of a bio-molecule. I invented several new pulse sequences, such as, R2TR and DARR for 13C-13C dipolar recoupling under MAS. After being promoted to a full Professor at 2006, I emphasize development of hardware and also start to study high-resolution methods for integer as well as half-integer quadrupolar nuclei. At present, I work as a member of the committee both in The Nuclear Magnetic Resonance Society of Japan and The Society of Solid-State NMR for Materials.

For phD study (1979 to 1984), my research interest was in structural organic chemistry, especially, steric strain in overcrowded molecules. I synthesized several model compounds having a methyl group in crowded environment and determined its activation energy for rotation in solids. For determination, I observed 1H spin-lattice relaxation using a so-called wideline NMR spectrometer. After PhD study, I took a Post-Doc position under Prof. C.A. McDowell at British Columbia University (Canada). I studied hydrogen bonding in keto-enol syetems by measuring 13C shielding tensors using a single crystal sample. Further, I developed several new methods (pulse sequences). Some of the sequences (TAPF and TREV) are still frequently used/cited in recent papers. After spending approximately 2.5 years in Canada, I moved to Berkeley to work with Prof. A. Pines as a Post-Doc. At Berkeley, I learned how to start a new thing by doing zero-field NMR and Xenon-NMR. At the end of 1986, I returned to Japan, and started working as a researcher at Foundation of Material Science and Technologies in Tokyo. After working approximately for 0.5 year, I moved to Department of Polymer Science, Faculty of Science, Hokkaido University as an Assistant Professor. After spending 5 years at Hokkaido studying mainly on polymer-blends, I came back to Kyoto University as an Associate Professor to work with Prof. Terao. In Kyoto, I started to develop solid-state NMR methods for determination of structure of a bio-molecule. I invented several new pulse sequences, such as, R2TR and DARR for 13C-13C dipolar recoupling under MAS. After being promoted to a full Professor at 2006, I emphasize development of hardware and also start to study high-resolution methods for integer as well as half-integer quadrupolar nuclei. At present, I work as a member of the committee both in The Nuclear Magnetic Resonance Society of Japan and The Society of Solid-State NMR for Materials.

Research Interests: Our main focus lies on the integration of microfluidic lab-on-a-chip technology with NMR spectroscopy and imaging. We believe that there is great potential for NMR in the context of LoC devices, due to its versatility, resolution, and non-invasive nature, which make it an ideal tool to study complex living systems. In addition, we are also interested in the behaviour of complex materials. Recent examples of this include polyelectrolyte hydrogels and brick-and-mortar type micro-composites. Vita: Marcel obtained a MSc in materials science from ETH Zürich in 1994. He then joined the research groups of Prof. Ueli Suter in Polymer Science, and of Prof. Richard R. Ernst in Physical Chemistry at ETH as a doctoral candidate. In 1998, he obtained his doctorate, with a thesis on solid-state NMR investigations of glassy polymers under plastic deformation. In 1999, he joined the group of Prof. Pablo DeBenedetti at Princeton University as a postdoc, with a stipend from the Swiss National Science Foundation. A year later, he joined the Institute of Materials Science and the Department of Physics at the University of Connecticut as an Assistant Professor. He was promoted to Associate Professor with Tenure in 2006. In the same year, he moved to the University of Virginia, where he joined the department of Mechanical and Aerospace Engineering. In 2012, Marcel moved to the UK, joining the School of Chemistry at the University of Southampton. He was promoted to a personal chair in 2014. He currently heads the section of Magnetic Resonance within the School of Chemistry. Marcel lives in Winchester, UK, with his wife Song and their son KangKang.

Research Interests: Our main focus lies on the integration of microfluidic lab-on-a-chip technology with NMR spectroscopy and imaging. We believe that there is great potential for NMR in the context of LoC devices, due to its versatility, resolution, and non-invasive nature, which make it an ideal tool to study complex living systems. In addition, we are also interested in the behaviour of complex materials. Recent examples of this include polyelectrolyte hydrogels and brick-and-mortar type micro-composites. Vita: Marcel obtained a MSc in materials science from ETH Zürich in 1994. He then joined the research groups of Prof. Ueli Suter in Polymer Science, and of Prof. Richard R. Ernst in Physical Chemistry at ETH as a doctoral candidate. In 1998, he obtained his doctorate, with a thesis on solid-state NMR investigations of glassy polymers under plastic deformation. In 1999, he joined the group of Prof. Pablo DeBenedetti at Princeton University as a postdoc, with a stipend from the Swiss National Science Foundation. A year later, he joined the Institute of Materials Science and the Department of Physics at the University of Connecticut as an Assistant Professor. He was promoted to Associate Professor with Tenure in 2006. In the same year, he moved to the University of Virginia, where he joined the department of Mechanical and Aerospace Engineering. In 2012, Marcel moved to the UK, joining the School of Chemistry at the University of Southampton. He was promoted to a personal chair in 2014. He currently heads the section of Magnetic Resonance within the School of Chemistry. Marcel lives in Winchester, UK, with his wife Song and their son KangKang.

S. Van Doorslaer has a long experience in conducting research on state-of-the-art pulsed EPR instruments, an experience she gained during her 6-years post-doctoral stay at ETH Zurich (Switzerland). Since 2012, she is professor at the University of Antwerp (Belgium), applying EPR to characterize biosystems and materials. She is one of the promoters of the UAntwerp Centre of Excellence ‘CASCH – Catalysis for sustainable organic chemistry’ and is currently president of the European Federation of EPR groups. She received the 2018 Bruker Prize of the ESR Spectroscopy Group of the Royal Society of Chemistry.

S. Van Doorslaer has a long experience in conducting research on state-of-the-art pulsed EPR instruments, an experience she gained during her 6-years post-doctoral stay at ETH Zurich (Switzerland). Since 2012, she is professor at the University of Antwerp (Belgium), applying EPR to characterize biosystems and materials. She is one of the promoters of the UAntwerp Centre of Excellence ‘CASCH – Catalysis for sustainable organic chemistry’ and is currently president of the European Federation of EPR groups. She received the 2018 Bruker Prize of the ESR Spectroscopy Group of the Royal Society of Chemistry.

Hervé Vezin has been CNRS Research Director at the Laboratory of Infrared and Raman Spectrochemistry (LASIR) since 2010. He was born on May 26, 1966 in Grenoble. After a master's degree in molecular biophysics at Pierre and Marie Curie University, he obtained a doctorate in molecular biophysics at the same university in 1995. He joined the CNRS in 1999 as a research associate and became Director of Research in 2005. In 2010 he became Deputy Director of LASIR and took over the presidency of the French Association of EPR until 2015 when he became Director of LASIR and the National EPR Infrastructure (RENARD). Hervé Vezin works on the magneto-structural properties of materials in the field of energy, catalysis, cosmo-chemistry in relation with the origin of life, and more generally in the field of materials chemistry with original developments in EPR spectroscopy and imaging.

Hervé Vezin has been CNRS Research Director at the Laboratory of Infrared and Raman Spectrochemistry (LASIR) since 2010. He was born on May 26, 1966 in Grenoble. After a master's degree in molecular biophysics at Pierre and Marie Curie University, he obtained a doctorate in molecular biophysics at the same university in 1995. He joined the CNRS in 1999 as a research associate and became Director of Research in 2005. In 2010 he became Deputy Director of LASIR and took over the presidency of the French Association of EPR until 2015 when he became Director of LASIR and the National EPR Infrastructure (RENARD). Hervé Vezin works on the magneto-structural properties of materials in the field of energy, catalysis, cosmo-chemistry in relation with the origin of life, and more generally in the field of materials chemistry with original developments in EPR spectroscopy and imaging.

+33 320336427

My research is focused on the development and translation of advanced MRI techniques for human studies including 7T MRI, MR spectroscopic imaging and hyperpolarized carbon-13 MRI. Main applications include cancer and brain disorders.

My research is focused on the development and translation of advanced MRI techniques for human studies including 7T MRI, MR spectroscopic imaging and hyperpolarized carbon-13 MRI. Main applications include cancer and brain disorders.

PhD in Physical Chemistry (solid-state NMR of functionalized materials, DFT), Postdoc in biological solid-state NMR, Habilitation in Physical Chemistry, Professor of Magnetic Resonance for Complex Materials and Catalysts

PhD in Physical Chemistry (solid-state NMR of functionalized materials, DFT), Postdoc in biological solid-state NMR, Habilitation in Physical Chemistry, Professor of Magnetic Resonance for Complex Materials and Catalysts