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Home  Invited Speakers
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Invited Speakers |
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| Confirmed Plenary Speakers | | |  | Cheryl Arrowsmith,University of Toronto, Canada
Cheryl Arrowsmith is a Senior Scientist at the Ontario Cancer Institute and Professor in the Department of Medical Biophysics at the University of Toronto. She is also the Chief Scientist of the Toronto Site of the Structural Genomics Consortium (SGC), and a member of the Northeast Structural Genomics Consortium (NESG). She received her Ph.D. in chemistry from the University of Toronto, and carried out postdoctoral research at Stanford University where she applied NMR spectroscopic methods toward understanding protein structure and function. Dr. Arrowsmith research uses structural and chemical biology methods to understand the structure-function relationships of proteins involved in cancer, epigenetics and transcriptional regulation. She is developing and applying these methods on a genome-wide scale. Dr. Arrowsmith is the holder of a Canada Research Chair in Structural Proteomics at the University of Toronto.
|  | Rolf Grütter,EPFL, Switzerland Rolf Grutter the Director of the Centre d’imagerie biomedicale and Head, Laboratory for functional and metabolic imaging (LIFMET). Most of the past research accomplishments have focused on developing magnetic resonance and applying the method to biomedical problems of importance.
Specifically, the pioneering advances in MR physics and engineering pioneered contributed to the recognition of the advantage of higher magnetic fields and include, but are not limited to (1) A fast field mapping method –important for the demonstration of the utility of high magnetic fields for in vivo investigation, now in several commercial scanners used to correct for susceptibility-induced BO distortions; (2) Establishment of the neurochemical profile - the simultaneous detection of more than 20 compounds in the brain; (3) Mathematical model of brain metabolism – establishing rigorous mathematical framework from which to derive quantitative metabolic rates in the live brain. A number of firsts resulted from such advances, among which are (1) direct measurement of brain glucose & its transport in human brain; (2) detection and measurement of glutamine synthesis in brain in vivo; measurement of the antioxidants, (3) glutathione and vitamin C in the brain; (4) Measurement of brain glycogen metabolism and content in vivo. These pioneering advances, among others, have lead to important novel insights, such as (1) The quantitative measurement of glutamate neurotransmission being a substantial metabolic flux in vivo. (2) Anaplerotic metabolism in brain in vivo (CO2 fixation) is important and quantitatively substantial. (3) Brain glycogen is present in substantial amounts and a relevant emergency energy reservoir in condition of glucose-deprivation, such as hypoglycemia, an important complication in diabetes. (4) Astrocyte (glial) energy metabolism is substantial and most ATP synthesis occurs by oxidative metabolism.
Overall, Dr. Gruetter’s research accomplishments and agenda illustrate the desire to bring closer together fundamental (exact) science with biomedical applications and problems. His pioneering contributions have opened many research areas and are well recognized by peers in magnetic resonance, neurochemistry and diabetes research.
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| Wolfgang Lubitz, MPI für Bioanorganische Chemie, Germany
Wolfgang Lubitz received his doctoral degree in chemistry at the Free University of Berlin in 1977. He worked as a Max Kade Fellow in the department of physics at UC San Diego (1983-1984), and as assistant and associate professor at the FU Berlin and at the University of Stuttgart, before he joined the faculty of the Technical University Berlin as full professor of physical chemistry in 1991. Since 2000 he is a Scientific Member of the Max Planck Society and Director at the Max Planck Institute for Bioinorganic Chemistry (formerly Radiation Chemistry) in Mülheim/Ruhr. He is Honorary Professor at the University of Düsseldorf. Since 2004 he is member of the council of the Meeting of Nobel Laureates in Lindau (Germany). From 2005 to 2008 he has been President of the International EPR/ESR Society.
Among other awards and fellowships he received the Zavoisky Award (Russia, 2002), the Bruker Prize (UK, 2003), the Gold Medal of the International EPR Society (2005) and recently a honorary doctorate of the University Uppsala (Sweden). He is a Fellow of the Royal Society of Chemistry (UK) and the International Society of Magnetic Resonance.
He is (co)author of about 300 publications in scientific journals. His group has contributed to the understanding of organic radicals and transition metal complexes as well as the structure and function of photosynthetic reaction centers and various metalloenzymes like ribonucleotide reductase, wateroxidase and hydrogenase. An important aspect of his work is the development and application of advanced EPR methods supplemented by quantum chemical calculations and other spectroscopic techniques.
|  | Beat Meier, ETH Zürich, Switzerland Beat Meier - 56 years, 2 childeren, Swiss nationality. Diploma in Chemistry 1998 from ETH Zürich, PhD 1984 from ETH Zurich under the direction of Prof. R.R.Ernst on solid-state NMR, Postdoctoral Fellow 1984 – 1986 at Los Alamos National Laboratory (USA) in the group of Dr. W.L. Earl. Methodical developments in high-res¬olution solid-state NMR spectroscopy, studies of dynamical proc¬esses in the solid, supercomputer simulations of spin dynamics. Staff scientist 1986-1994 Laboratorium für physikalische Chemie of the Swiss Federal Institute of Technology, Zurich, in the research group of Prof. R.R. Ernst. Research activities in the field of solid-state NMR spectroscopy, with a focus on methodological developments in solid-state NMR, in particular the development of new tools for structure determination in microcrystalline and non-crystalline compounds. Habilitation 1993, Department of Chemistry ETH Zurich, Title of the Habilitation thesis: Polarization Transfer and Spin Diffusion. Full professor in Physical Chemistry 1994-1998 at the University of Nijmegen (The Netherlands) and member of the board of the Nijmegen SON Research Center for Molecular Structure, Design and Synthesis and of the board of the National High-Field NMR facility.
Since 1998 Full professor in Physical Chemistry at the Department of Chemistry and Applied Biosciences. Research topics include: methodological developments in solid-state NMR, dynamics and thermodynamics of spin systems under multiple pulses and sample rotation. Application of solid-state NMR to high-resolution structure determination and the investigation of dynamical processes in biosolids. Study of the local structure of macroscopically disordered systems (biopolymers, polymers and polymer blends, glasses, dynamically disordered systems). Magnetic resonance force detection and NMR imaging at the nanoscale. Head of the department of Chemistry and Applied Biosciences 2008.
|  | Masahiro Shirakawa, Kyoto University, Japan Masahiro Shirakawa - Research and professional experience:
1988 July-December Post doctoral fellow at Institute of Protein Research, Osaka University, supported by Japan Society for the Promotion of Science
1989-1995 Research Associate, Institute of Protein Research, Osaka University
1995-2001 Associate Professor, Nara Institute of Science and Technology
2001-2004 Professor, Yokohama City University
2005-present Professor, Kyoto University
|  | Gerhard Wagner, Harvard University, USA Gerhard Wagner - is the Elkan R. Blout Professor in the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School.
Gerhard Wagner studied Physics at the Technical University in Munich. He obtained his Ph.D. from the ETH Zürich in 1997 under Kurt Wüthrich with NMR studies of protein internal mobility. After a short visit at MIT he returned to the ETH where he developed methods for protein resonance assignment and structure determination. From 1987 to 1990 he was a faculty at the University of Michigan where he developed triple-resonance methods for protein assignments. In 1990 he moved to Harvard Medical School. His current interests are on structural biology of gene expression, eukaryotic translation initiation, immunology and apoptosis. He is also intersted in membrane protein structures and small molecule inhibitors of protein-protein interactions.
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| Peter Wright, The Scripps Research Institute, USA
Peter E. Wright is Professor and Chairman of the Department of Molecular Biology and holds the Cecil and Ida Green Chair of Biomedical Research at the Scripps Research Institute, California, USA. He received B.Sc., M.Sc. and Ph.D. degrees from the University of Auckland, New Zealand, and undertook postdoctoral studies at Oxford University, UK, from 1972–1976. He joined the faculty at the University of Sydney, Australia in 1976. He was appointed to the faculty of Scripps in 1984 as Professor, and became Chairman of the Department of Molecular Biology in 1987.Dr. Wright has been Editor-in in-Chief of the Journal of Molecular Biology since 1990. His lab is focused on the applications of NMR to protein folding and intrinsically disordered proteins, solution structure determination and dynamic studies of proteins, and protein–nucleic acid interactions.
Dr. Wright is an elected fellow of several professional societies including the International Society of Magnetic Resonance, NMR Society of Japan, the American Academy of Arts and Sciences, and the American Association for the Advancement of Science, and is a member of the National Academy of Sciences.
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| Kurt Wüthrich, The Scripps Research Institute, USA
Kurt Wüthrich is the Cecil H. and Ida M. Green Professor of Structural Biology at The Scripps Research Institute, La Jolla, CA, USA, and Professor of Biophysics at the ETH Zürich, Zürich, Switzerland. His research interests are in structural biology and structural genomics. His specialty is nuclear magnetic resonance (NMR) spectroscopy with biological macromolecules, where he contributed the NMR method of three-dimensional structure determination of proteins and nucleic acids in solution. Kurt Wüthrich’s achievements have been recognized by the Prix Louis Jeantet de Médecine, the Kyoto Prize in Advanced Technology, the Nobel Prize in Chemistry, and by a number of other awards and honorary degrees.
| | | | | Confirmed Keynote Speakers | | |  | Hideo Akutsu, Osaka University, Japan
He was appointed as an instructor at Osaka Univ in 1972, moved to Yokohama National Univ in 1985 as an associate professor and then became a full professor in 1991. He moved back to IPR, Osaka Univ in 2000 and became professor emeritus in 2007. He is the president of NMR Society of Japan from 2008. His research interest is elucidation of the mechanism of energy conversion systems such as H+-ATPsynthase at the membrane interfaces, using solution and solid-state NMR.
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| Frédéric Allain, ETH Zürich, Switzerland
Frédéric Allain was born in France in 1969. He studied chemistry at the Ecole Normale Superieure in Paris and did his PhD with Dr. G.Varani at the MRC-LMB of Cambridge where he determined one of the first protein-RNA complex structures using NMR (1993-1997). Between 1997 and 2000, he was a Postdoctoral Fellow at UCLA in the group of Prof. J.Feigon, followed by one year as Research associate in the HHMI/UCLA in the group of Prof. D.Black.
In August 2001, Frédéric Allain joined the Institute of Molecular Biology and Biophysics of the ETH Zürich initially as an Assistant Professor and in 2007 became an Associate Professor. Prof. Allain’s research interest is centered around understanding the molecular mechanisms involved in the regulation of several post-transcriptional gene regulation processes namely RNA editing, RNA alternative-splicing and translation regulation. To this aim, Prof. Allain’s group has determined using NMR several structures of RNAs, proteins and protein-RNA complexes associated with these processes.
|  | Lucia Banci, University of Florence, Italy
Lucia Banci is Professor of Chemistry at the University of Florence. Her research expertise is focused on structural biology in solution, through high resolution NMR spectroscopy, to which she has contributed in methodological and theoretical advancements. She is an active player in Structural Genomics projects. Her approach is driven by the “function perspective” more than by a broad coverage of the genome products. She is focusing on proteins involved in a few pathways responsible of copper homeostasis. She is providing unique contributions to the understanding of the processes of copper transport in the cell and its incorporation into the final targets. Within this frame, she is also addressing the weak, transient protein-protein interactions which are at the basis of a large number of biological processes. Finally, she is characterizing proteins which are naturally unstructured or partially unfolded. She has published over 270 research articles and has solved about 50 protein structures.
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| Ad Bax, NIH, USA
Ad Bax was born in 1956, in The Netherlands. In 1981, he received his Ph.D. in Applied Physics from the Delft University of Technology for work on the development of two-dimensional nuclear magnetic resonance (NMR) techniques, which he carried out at Delft and Oxford Universities. His PhD thesis was republished in book format, and for many years was the standard text for new researchers entering this field. During a post-doctoral research stint at the National NMR Facility in Fort Collins, Colorado, he introduced the now classic magic angle flipping and hopping experiments, which allow detailed chemical information to be extracted from solid materials. He joined the National Institutes of Health in 1983, where he developed an array of powerful NMR experiments that are now being used widely for the study of the three-dimensional structure and dynamic properties of proteins and nucleic acids. He is a corresponding member of the Dutch Royal Academy of Sciences, a competing member of Artemis Racing, and a member of the National Academy of Sciences, USA.
|  | Rolf Boelens, Utrecht University, Netherlands
Rolf Boelens studied chemistry and physical chemistry at the University of Groningen, The Netherlands. He completed his Ph.D. on EPR of cytochrome c oxidase in the Department of Biochemistry of the University of Amsterdam in 1984. For a postdoc he went to the NMR group of Robert Kaptein, and in 1988 he was appointed assistant professor at the Faculty of Chemistry, Utrecht University, The Netherlands. Currently he is professor of biomolecular NMR spectroscopy and director of the European NMR facility at Utrecht University. His research interests are biomolecular interactions with an emphasis on transcription and DNA repair. Studied systems have been the DNA binding domains of lac and other repressors, steroid hormone receptors and DNA repair proteins, and enzymes such as phospholipase A2 and subtilisine. A series of computational methods are applied and developed, such as restrained molecular dynamics and iterative relaxation matrix refinement (IRMA) for structure determination. His research has resulted in ca. 300 publications. |  | Teresa Carlomagno, EMBL Heidelberg, Germany Teresa Carlomagno - was born in Italy and studied Chemistry at the University of Naples Federico II. She obtained her Ph.D. from the same University in 1996. After obtaining the Ph.D. she joined the University of Frankfurt, Germany, where she spent 2,5 year as a postdoc. She was research assistant at the The Scripps Research Institute in California from 2000 to 2001 and in 2002 she became an independent research Group Leader at the Max Planck Institute for Biophysical Chemistry in Göttingen, Germany. Currently she holds the position of group leader in Biomolecular NMR Spectroscopy at the EMBL in Heidelberg, Germany.
Her research group investigates the structural basis of intermolecular interactions and RNA folding by nuclear magnetic resonance spectroscopy in solution with a special focus on RNA processing complexes and mechanisms of anticancer drugs activity. Additionally, her group develops novel NMR techniques for structural investigation of biomolecules and drug design.
|  | Marius Clore, NIH, USA
Marius Clore is Chief of the Protein NMR Section at the NIH (1988-present). He received his MD and PhD degrees at University College Hospital Medical School and the MRC National Institute for Medical Research in London, and was joint Head of the Biological NMR group at the Max Planck Institute for Biochemistry in Munich (1984-1988). His major research interests lie in the application of NMR spectroscopy to study the structure and dynamics of macromolecular complexes.
|  | Tim Cross, Florida State University, USA Timothy Cross - b 1953. B.S., 1976, Chemistry, Trinity College, Hartford, CT. (undergraduate research with H. DePhillips), Ph.D. 1981, Chemistry, University of Pennsylvania (with S.J. Opella), postdoctoral fellow 1981-1983 with S. J. Opella and 1983-1984 with J. Seelig, University of Basel, Switzerland. Professor of Chemistry and Biochemistry, Florida State University 1984-present, Director of the NMR Spectroscopy and Imaging Program at the National High Magnetic Field Laboratory 1998-present. Approx. 185 publications. Research interests: solid state and solution NMR spectroscopy of membrane proteins, dynamics, structural and functional elucidation, special interest in the membrane proteins of Influenza A and Mycobacterium tuberculosis. |  | Chris Dobson, University of Cambridge, UK Chris Dobson - Professor Chris Dobson received his doctorate from the University of Oxford in 1976, having worked on the application of chemical and physical techniques to probe the structures and dynamics of biological molecules, particularly proteins.
After a short period as a Research Fellow he moved to Harvard University as an Assistant Professor of Chemistry, and was also a Visiting Scientist at MIT. In 1980 he returned to the University of Oxford first as a Lecturer in Chemistry and later as Professor of Chemistry and Director of the Oxford Centre for Molecular Sciences.
In 2001 he moved to the University of Cambridge as John Humphrey Plummer Professor of Chemical and Structural Biology. In 2007 he was awarded the degree of ScD by the University and in the same year became Master of St John's College, Cambridge.
Chris Dobson was elected a Fellow of the Royal Society in 1996 and of the Academy of Medical Sciences in 2005. In 2007 he was elected to Honorary Foreign Membership of the American Academy of Arts and Sciences. He has received many awards during his career including the Stein and Moore (2003) and the Hans Neurath (2006) Awards of the Protein Society, and the Davy Medal of the Royal Society (2005). He has also been awarded four Honorary Degrees in Science and Medicine. In 2009 he was awarded the Royal Medal by the Royal Society "for his outstanding contributions to the understanding of the mechanisms of protein folding and mis-folding, and the implications for disease."
His research interests are increasingly focused on defining the way that protein molecules fold up into the compact structures in which they function. More recently his work has been directed towards an understanding of the failure of proteins to fold correctly under some circumstances, and its consequences as the origin of human disorders such as Alzheimer’s disease and diabetes.
He published over 500 papers and review articles in total, including more than 30 in Nature and Science. 150 of these publications are within the last five years. Current h-index (based on citations) is 99.
|  | Jane Dyson, The Scripps Research Institute, USA
Jane Dyson received the degree of B.Sc.(hons) from the University of Sydney in 1973 and a Ph.D. from the University of Sydney in 1977, under the direction of James Beattie. She was a postdoctoral fellow at Massachusetts Institute of Technology under the direction of Paul Schimmel from 1977-78, and held a Damon Runyon-Walter Winchell postdoctoral award. She was appointed as a Lecturer in Chemistry at the University of New South Wales in 1979, and joined the Scripps Research Institute in 1984, where she is presently a Professor. Her research interests are in the conformation of peptides, protein folding and dynamics, and structure and functional studies of proteins using NMR and other spectroscopic techniques.
|  | Kevin Gardner, UT Southwestern, USA
Kevin Gardner is the Virginia Lazenby O’Hara Chair in Biochemistry and W.W. Caruth Jr. Scholar in Biomedical Research at the UT Southwestern Medical Center in Dallas. After obtaining his undergraduate training at UC Davis (Biochemistry; 1989), he began working in the area of biomolecular NMR via Ph.D. studies with Joe Coleman in the Molecular Biophysics & Biochemistry department at Yale (1989-1995). From here, he joined Lewis Kay’s group at the University of Toronto for postdoctoral research (1995-1998). While there, he developed a combination of biochemical, biophysical and computational tools to extend the ability of solution NMR methods to study the structure and dynamics of larger proteins. In 1998, Dr. Gardner joined the departments of Biochemistry and Pharmacology at the University of Texas Southwestern Medical Center in Dallas, where he is currently a Professor in these departments. His research group integrates structural, dynamic and kinetic information from solution NMR studies with results from other biophysical and biochemical methods to probe the signaling mechanisms of environmental sensory proteins. The long-term goals of this research are to understand how related protein folds can be harnessed to sense different environmental stimuli – e.g. blue light, oxygen, organic compounds – to control different output functions. In doing so, such studies lay the foundation for both understanding the natural regulation of these systems and their artificial control of engineered proteins.
|  | Christian Griesinger, MPI für Biophysikalische Chemie, Germany Christian Griesinger - Christian Griesinger studied chemistry and physics at the University of Frankfurt (1979-84) and obtained his PhD also there with Horst Kessler in 1986. He was a postdoctoral fellow at ETH Zürich with Richard R. Ernst from 1986-1989 and then moved to a full professor position at the university of Frankfurt in 1990. He was made director and scientific member of the Max Planck Institute for Biophysical Chemistry in Göttingen in 1999 and moved there in 2001. Research interests are in the field of method developments in NMR spectroscopy and its application to structure, dynamics, reactions and dynamics of biomolecules. Further interest lies in the determination of configuration of small molecules and sensitivity enhancement of NMR spectroscopy, structural biology of neurodegeneration and enzyme mechanisms. Some of the work has been published in 245 publications until the present day. |  | Peter Güntert, University of Frankfurt, Germany
Professor Peter Güntert was born in 1964 in Schaffhausen, Switzerland. In 1987, he received his masters in science (Diploma in physics) at ETH Zurich. He received his Ph.D in 1993 at the same institution under the advisors of Kurt Wüthrich and Wilfred F. van Gunsteren. 1998 saw Professor Güntert achieve habilitation in Mathematics and Physics at ETH Zurich. In 1986 his career started as a high school teacher in Mathematics and and computer science; he then moved on to be a predoctoral and postdoctoral researcher at the Institute of Molecular Biology and Biophysics, ETH Zürich from 1988 to 1995. After becoming a senior researcher and lecturer from 1996 to 2002, Professor Güntert moved organisations and began employment at RIKEN Yokohama Institute in Japan. He finished his role as a team leader in NMR Structure Analysis Methodology Team in 2007 and until now is a Professor at the Institute of Biophysical Chemistry, Goethe-University Frankfurt am Main; Fellow at the Frankfurt Institute of Advanced Studies (FIAS), Frankfurt am Main; and a visiting Professor at the Department of Chemistry, Tokyo Metropolitan University.
|  | Horst Kessler, Technische Universität München, Germany
Horst Kessler studied Chemistry in Leipzig and Tübingen (1958-1966) and became full professor of Organic Chemistry at the Goethe University in Frankfurt in 1971. 1989 he moved to the Technische Universität München were he now is Carl von Linde Professor at the Institute for Advanced Study. His interest went from small molecule NMR to peptide and protein NMR. He developed and used multidimensional NMR techniques mainly for cyclic peptides and proteins. In addition he is active in drug development of peptides and peptidomimetics based on conformational design and synthesis, highlighting in the development of the drug cilengitide which is now in clinical phase III (Merck KGaA Darmstadt). His NMR interest is now in the field of p53 interactions, heat shock proteins, and recently in spider silk domains. Horst Kessler published more than 650 scientific papers. He won a number of awards, among them the Otto-Bayer-Preis (1986), Emil-Fischer-Medal (1997), the Max-Planck-Forschungspreis (2001), Philip Morris Research Award (2003), Vincent Du Vigneaud Award of the American Peptide Society and the Josef Rudinger Award of the European Peptide Society. He is member of the German Academy of Science Leopoldina, the Bayerische Akademie der Wissenschaften, honorary member of the Israel Chemical Society and the NMR Society of India and recieved an honorary doctorate from the University of Leipzig. |  | Francesca Marassi, Burnham Research Institute for Medical Research, USA
Francesca Marassi earned her Ph.D. in Chemistry from the University of Toronto in 1993. She received postdoctoral training at the University of Pennsylvania from 1993 to 1998, where she held Fellowships from the Natural Sciences & Engineering Research Council of Canada and the Medical Research Council of Canada (1995-1998). From 1998 to 2000, she was Assistant Professor at the Wistar Institute in Philadelphia, and she is currently on the faculty of the Burnham Institute in La Jolla. Her research focuses on the application of NMR to membrane-associated proteins.
|  | John Markley, University of Wisconsin-Madison, USA
John Markley has spent his entire scientific career in the field of biomolecular NMR spectroscopy. He received his Ph.D. degree from the Biophysics Program at Harvard University. His first publication documented the upfield shift of the alpha proton of polyaminoacids upon transition from random coil to alpha-helix, a study carried out at 60 MHz. The last three years of his thesis work with Oleg Jardetzky on selective deuteration as a means for simplifying NMR spectra and making assignments was carried out at the Merck Research Institute with a 100 MHz NMR spectrometer. Markley was an NIH postdoctoral fellow with the late Mel Klein at the University of California, Berkeley, where he learned the then new technique of Fourier transform NMR spectroscopy and applied it to studies of phosphorus-31 relaxation. He set up an independent laboratory in the Chemistry Department at Purdue University, where he was hired as an Assistant Professor, and later progressed to Professor and Chair of the Biochemistry Division. While at Purdue, he and his group used NMR to investigate enzyme reaction mechanisms and interactions between serine proteases and inhibitors. They also carried out early one- and two-dimensional NMR studies of carbon-13 and nitrogen-15 labeled proteins. Markley was recruited to Biochemistry Department the University of Wisconsin-Madison in 1984, where he now is the Steenbock Professor of Biomolecular Structure. He heads the National Magnetic Resonance Facility at Madison, supported by the National Center for Research Resources, and the Biological Magnetic Resonance Data Bank (BMRB), supported by the National Library of Medicine. In addition, he directs the Center for Eukaryotic Structural Genomics. His current interests are in the fields of structural genomics, metabolomics, and iron-sulfur protein chemistry.
|  | James Prestegard, University of Georgia
James H. Prestegard received a Ph.D. in chemistry from Caltech in 1971. He moved directly to a faculty position in the Chemistry Department of Yale University where he stayed through 1997. In 1998 he moved to the University of Georgia where he is Professor and Eminent Scholar in Nuclear Magnetic Resonance Spectroscopy. He conducts research in the Complex Carbohydrate Research Center at the University of Georgia and contributes to teaching in the Chemistry and Biochemistry Departments. His research interests center on the application of Nuclear Magnetic Resonance to structural characterization of biomolecules, including proteins, carbohydrates and membrane assemblies. His research has received recognition through election as a Fellow of the American Association for the Advancement of Science, election as a Fellow of the Biophysical Society, election as a Fellow of the International Society for Magnetic Resonance, and award of the 2002 Laukien Prize for Experimental Magnetic Resonance Spectroscopy (joint with A. Bothner-By and A. Bax). He has administrative responsibilities for a Research Resource for Integrated Glycotechnology and the Southeast Collaboratory for Biomolecular NMR (900 MHz).
|  | Rob Tycko, NIH, USA
Robert Tycko is a member of the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases of the U.S. National Institutes of Health. Years ago, he was the sole inventor of zero field NMR in high field, a technique that has never been used. Tycko's oeuvre includes solid state NMR investigations of Berry's phase, high-temperature ceramic and fullerene superconductors, two-dimensional electron systems in semiconductor quantum wells, AIDS-related proteins, and amyloid fibrils. He still works on pulse sequences. He also dabbles in electron microscopy.
|  | Mingjie Zhang, Hong Kong University of Science and Technology, Hong Kong
Mingjie Zhang is a Chair Professor in the Department of Biochemistry at the Hong University of Science & Technology. His research interest is in the molecular basis of protein complexes regulating neuronal signal transduction and controlling cell polarity. Dr. Zhang has published extensively in the leading journals including Science, Mol Cell, Nature Structural Biology/Nature Structural & Molecular Biology, EMBO J, etc. Dr. Zhang has been very successful in attracting basic research grants both from local (e.g., Research Grant Council of Hong Kong) and international (e.g., Human Frontier Science Program) grant agencies. In 2003, Dr. Zhang was awarded as a Croucher Senior Fellow and an Outstanding Young Scientist by the National Science Foundation of China for his excellent research achievement. In 2006, Dr. Zhang won the State Natural Science Award, which is the most prestigious award in the areas of science and technology in China.
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Confirmed Session Speakers
Jacob Anglister, Weizmann Institute of Science, Israel
| Martin Blackledge, Institut de Biologie Structurale Jean-Pierre Ebel, France | | Alexandre Bonvin, Utrecht University, Netherlands | Kevin Brindle, Cancer Research UK, UK | | David Britt, UC Davis, USA | Rafael Brüschweiler, Florida State University, USA | | Sam Butcher, University of Wisconsin–Madison, USA | Matthew Call, Harvard Medical School, USA | | Kandala Chary, Tata Institute, India | Byong-Seok Choi, Korea Advanced Institute of Science and Technology, S.Korea | Huub de Groot, Universiteit Leiden, The Netherlands
| Muriel Delepierre, Institut Pasteur, France
| | Volker Dötsch, University of Frankfurt, Germany | Juli Feigon, UCLA, USA | Robert Gillies, Moffitt Cancer Center, USA
| Steffen Glaser, Technische Universität München, Germany | | Angela Gronenborn, University of Pittsburgh, USA | Stephan Grzesiek, University of Basel, Switzerland | Judith Herzfeld, Brandeis University, USA
| Song-I Han, UCSB, USA
| Mei Hong, Iowa State University, USA
ICMRBS Founders' Medallist | Ramakrishna Hosur, Tata Institute of Fundamental Research, India | Tai-Huang Huang, Academia Sinica, Taiwan | Mitsu Ikura, University of Toronto, Canada | | Fuyuhiko Inagaki, Hokkaido University, Japan | Yoshitaka Ishii, University of Illinois, USA
| | Naranamangalam Jagannathan, All India Institute of Medical Sciences, India | Wolfgang Jahnke, Novartis, Switzerland | | Gunnar Jeschke, ETH-Zürich, Switzerland | Michael Kennedy, Miami University, USA
| | Dorothee Kern, Brandeis University, USA | Jun Kikuchi, RIKEN, Japan | | Alan Koretsky, NIH, USA | Claudio Luchinat, University of Florence, Italy | | Georges Mer, Mayo Clinic, USA | Anthony Mittermaier, McGill University, Canada | Niels Nielsen, University of Aarhus, Denmark
| Daniel Nietlispach, University of Cambridge, UK | | Michael Nilges, Pasteur Institute, France | Stanley Opella, UCSD, USA | | Vladislav Orekhov, University of Gothenbur, Sweden | Art Palmer, Columbia University, USA | | Arthur Pardi, University of Colorado at Boulder, USA | Maurizio Pellecchia, Burnham Institute for Medical Research, USA | | Thomas Prisner, University of Frankfurt, Germany | Scott Prosser, University of Toronto at Mississauga, Canada | | Bernd Reif, FMP Berlin, Germany | Peter Sadler, University of Warwick, USA | | Michael Sattler, Helmholtz Zentrum München, Germany | Jurgen Schleucher, Universitet Umea, Sweden | | Harald Schwalbe, University of Frankfurt, Germany | Yunyu Shi, University of Science and Technology of China, PRC | | Ichio Shimada, University of Tokyo, Japan | Thomas Szyperski, University at Buffalo, USA | | Kiyonori Takegoshi, Kyoto University, Japan | David Thomas, University of Minnesota, USA | | Vitali Tugarinov, University of Maryland, USA | Anne Ulrich, University of Karlsruhe, Germany | | Gabriele Varani, University of Washington, USA | Gianluigi Veglia, University of Minnesota, USA | | Michele Vendrusculo, University of Cambridge, UK | Brian Volkman, Medical College of Wisconsin, USA | | Mike Williamson, University of Sheffield, UK | David Wishart, University of Alberta, Canada | | Daiwen Yang, National University of Singapore, Singapore | Markus Zweckstetter, Max Planck Institute for Biophysical Chemistry, Germany |
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Last Updated ( Monday, 16 August 2010 )
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