Abstracts, addresses and Biographies
Professor Edvard Moser
Kavli Institute for Systems Neuroscience and Centre for Neural Computation, Norwegian University of Science and Technology (NTNU), Trondheim, Norway, email:edvard.moser@ntnu.no
Premises for a Nobel prize – how can infrastructure and support prepare the ground for breakthroughs in basic research?
Many university leaders have asked me what they should do to promote the growth of researchers who make discoveries that are significant enough to earn the Nobel Prize. Unfortunately, there is no simple answer to the question – and what is right may differ between scientific disciplines – but yet I do believe I can provide a few general clues, on the background of my own experiences. First of all, talent cannot be created de novo. If I were a university dean or rector, I would search around for the talents – every institution has some of them but finding the ones with the right combination of creativity, independence, motivation, dedication, persistence and interpersonal skills may take some work. Efforts should target those individuals. Second, breakthrough research takes time. Those with the potential for revolutionary discoveries have a vision. They have plans and ambitions that extend across decades – usually not following the mainstream. Funding and infrastructure must allow for out-of-the-box projects; a small number of identified candidates must be given time and financial security to reach their goals, not having to rely exclusively on conventional 3-5-year project grants. Third, identified candidates must be evaluated rigorously and regularly by the best peers in their fields. Success rates may be low and university leadership must be able to distinguish between those that may make it and those many that won¨t. Such decisions cannot be made based on numbers of publications; only in-depth progress evaluation by the best in the field can separate the wheat from the chaff.
Biography
Edvard Moser is a Professor of Neuroscience and Director of the Kavli Institute for Systems Neuroscience at the Norwegian University of Science and Technology in Trondheim. He is interested in how spatial location and spatial memory are computed in the brain. His work, conducted with May-Britt Moser as a long-term collaborator, includes the discovery of grid cells in the entorhinal cortex, which provides clues to a neural mechanism for the metric of spatial mapping. Subsequent to this discovery the Mosers have identified additional space-representing cell types in the entorhinal cortex and they are beginning to unravel how the neural microcircuit is organized. In addition to showing how a variety of functional cell types contribute to representation of self-location, they have shown what mechanisms underlie the computation of space, how the outputs of the circuit are used by memory networks in the hippocampus, and how episodic memories are separated from each other in the early stages of the hippocampal memory storage. The discovery of grid cells and their control of population dynamics in the hippocampus have led to a revision of established views of how the brain calculates self-position, and spatial mapping and is becoming one of the first non-sensory cognitive functions to be characterized at a mechanistic level in neural networks.
Edvard Moser received his initial training at the University of Oslo under the supervision of Dr. Per Andersen. He worked as a post-doc with Richard Morris and John O’Keefe in 1996, before he accepted a faculty position at the Norwegian University of Science and Technology the same year. In 2002 he became the Founding Director of the Centre for the Biology of Memory. In 2007 the Centre became a Kavli Institute. Edvard Moser is also Deputy Director of the newly established Centre for Neural Computation at the same institution. Together with May-Britt Moser, he has received a number of awards, including the 2014 Nobel Prize in Medicine or Physiology.
Professor G.J.M. Meijer
Fritz-Haber-Institut der Max-Planck-Gesellschaft Faradayweg 4-6, D-14195 Berlin-Dahlem, Germany, e-mail: meijer@fhi-berlin.mpg.de
Controlling molecular conformational distributions
In this presentation, an overview will be given of the methods that have been developed over almost a century to control the motion of neutral molecules in the gas-phase with electric fields [1]. This research dates back to the time that Odd Hassel performed his PhD research at the Kaiser Wilhelm Institute in Berlin-Dahlem, and was initiated at that same institute. The now matured methods for the manipulation of neutral molecules bear resemblance to the wellknown methods used for the control of charged particles and exploit the force that a neutral molecule with an electric dipole moment experiences in an inhomogeneous electric field. Analogous to the separation of ions based on their mass-to-charge ratios in a quadrupole mass filter, neutral conformers can be separated based on their different mass-to-dipole-moment ratios in an ac electric quadrupole selector [2]. I will also discuss how cold collisions catalyse conformational conversion in the expansion region of a molecular beam [3]. Via either one of these methods, conformer-selected samples of gas-phase molecules can be prepared, offering novel perspectives for a variety of experiments [4].
References: [1] S.Y.T. van de Meerakker, H.L. Bethlem, N. Vanhaecke, and G. Meijer, Chem. Rev. 112, 4828-4878 (2012).
[2] F. Filsinger, U. Erlekam, G. von Helden, J. Küpper, and G. Meijer, Phys. Rev. Lett. 100, 133003-1,133003-4 (2008).
[3] U. Erlekam, M. Frankowski, G. von Helden, and G. Meijer, PCCP 9, 3786-3789 (2007).
[4] Y.P. Chang, K. Dlugolecki, J. Küpper, D. Rösch, D. Wild, and S. Willitsch, Science 342, 98-101 (2013).
Biography
Gerard Meijer (1962) studied physics at Radboud University, Nijmegen, The Netherlands, where he also completed his PhD (1988). Subsequently, he worked for two years as an assistant researcher at IBM (San José, CA, USA). He then returned to Nijmegen where he was appointed full professor of experimental physics in 1995. In 2000 he became director of the FOM Institute for Plasma Physics in Nieuwegein, and in 2002 director of the Fritz Haber Institute (FHI) in Berlin, where he established the Molecular Physics department. In September 2012, he accepted the “call of duty” to serve as President of the Executive Board of the Radboud University in Nijmegen, a position that he held until the beginning of 2017. Since then, he has been reappointed as director of the FHI in Berlin. Since January 2018 he is elected member of the German Council of Science and Humanities (Wissenschaftsrat).
Gerard Meijer has received various awards for his scientific work and for his service to academia. In 2009 he received the Bourke Award from the Royal Society of Chemistry for his original research into the formation and spectroscopy of ultra-cold molecules. In 2010 he acquired an ERC Advanced Grant. In 2012, he was awarded the Van ’t Hoff Prize in Germany for his outstanding contributions to physical chemistry. In 2013 he was elected member of the Academia Europaea and in 2017 he received a royal decoration and became Knight in the Order of the Netherlands’ Lion.
Gerard Meijer has co-authored about 400 articles in refereed scientific journals that have received a total of over 22.000 citations; his h-index is 74. Fourty-five Ph.D. students have completed their Ph.D. research under his supervision.
( As you might know, Odd Hassel actually performed his PhD research at the Kaiser-Wilhelm-Institut in Berlin-Dahlem that I am working at right now, and Fritz Haber was an important mentor to him. In my presentation, I will therefore tell somewhat about the history of this KWI and on how Odd Hassel’s PhD research fits into this picture.)
Professor Thomas W. Ebbesen
Director of the University of Strasbourg Inst. for Advanced Studies, France, Thomas Ebbesen ebbesen@unistra.fr
The Alchemy of Vacuum - Hybridizing Light and Matter
Light-matter interactions are not only fundamental for the existence of life, such as we know it, but play a key role in our culture, in the exchange of information and in many tools from surgery to the making of cars. What is perhaps more surprising, is that light-matter interactions occur even in total darkness. This is because vacuum, the three-dimensional space in which we exist, is not a void but is full of quantum fluctuations, including electromagnetic fluctuations which affect for instance the forces between molecules. When such light-interactions become strong enough, a new regime arises characterized by the formation of hybrid light-matter states. This is the so-called strong coupling regime which leads to fundamental changes in material properties. After introducing some of the basic concepts, examples of modified material properties such as conductivity, energy transport and chemical reactivity will be presented.
Biography
Thomas W. Ebbesen is a physical chemist born in Oslo, Norway. He was educated in the United States and France, receiving his bachelor degree from Oberlin College (Ohio) and his PhD from the Curie University in Paris. He then did research in both the US and Japan, most notably at NEC Corporation, before returning to France in 1999 to help build a new institute at the University of Strasbourg. He is currently the head of the Center for Frontier Research in Chemistry and the Strasbourg Institute for Advanced Studies (www.usias.fr). He holds the chair of physical chemistry of light-matter interactions. The author of many papers and patents, Ebbesen has received numerous awards for his pioneering research on nanostructured materials including the 2014 Kavli Prize in Nanoscience for his transformative contributions to nano-optics. He is a member of the Norwegian Academy of Science and Letters, and a foreign member of the French Academy of Science and the Royal Flemish Academy of Belgium for Science and Arts.
Professor Laura Hartmann
Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, D-40225 Düsseldorf, Germany, e-mail: laura.hartmann@hhu.de
Biomimetic polymers – now available with sequence-control
Many of the advanced properties of modern synthetic polymers are inspired by nature and their natural counterparts, such as proteins or oligonucleotides. However, synthetic polymers have not yet attained the complexity and functionality of biopolymers e.g. the catalytic properties of enzymes or the information content of a DNA. The limiting factor here is not access to functional groups that can be incorporated into the polymer. Rather, they lack the precision in the arrangement of functional components, the so-called sequence control.
Our approach is based on the use of solid phase synthesis applying peptide coupling protocols to novel tailor-made building blocks in order to generate monodisperse, sequence-controlled macromolecules. Special focus has been devoted to the synthesis of glycofunctionalized, sequence-controlled macromolecules, so-called precision glycomacromolecules. They are used to study binding mechanisms in multivalent sugar-lectin interactions and address biological processes such as cell-cell interactions or pathogen recognition. The lecture will present the bottom-up synthesis of precision glycomacromolecules, starting from small building blocks, solid phase assembly of oligomers, going to higher molecular weight structures and will discuss their potential biomedical applications.
Biography
Laura Hartmann is a polymer chemist and holds the chair for Macromolecular Chemistry at the Heinrich-Heine-University (HHU) Düsseldorf in Germany. She finished her PhD under the supervision of Hans Börner and Markus Antonietti at the Max Planck Institute of Colloid and Interfaces (MPI KGF) Potsdam, Germany in 2007. Thereafter, she worked as a Research Fellow in the groups of Curtis Frank (Chemical Engineering) and Christopher Ta (Ophthalmology) at Stanford University, USA. In August 2009 she started her independent Emmy Noether research group on Polymeric Biomimetics at the MPI KGF within the Department for Biomolecular Systems headed by Peter Seeberger and the Freie Universität Berlin, Germany. In July 2014 she was appointed full professor at HHU Düsseldorf. Her research is focused on combining solid phase and polymer synthesis to obtain monodisperse, sequence-defined polymers. In particular, she is interested in the synthesis, characterization and application of glycopolymers and glycomaterials in biotechnology and biomedicine.
Professor Pekka Pyykkö
Department of Chemistry, University of Helsinki, P.O. Box 55 (A.I. Virtasen aukio 1), FIN-0001 University of Helsinki.
FINLAND, Phone: +358-2941 50171, pekka.pyykko@helsinki.fi
Some trends in the periodic table
The (pre)history of the Periodic Table (PT) is briefly discussed, starting from Döbereiner’s triads. In addition to Mendeleev’s 1869 publications, the secondary periodicity of Biron (1914) is mentioned. The first analysis of the Ytterby mineral by Gadolin (1794), leading to the identification of rare-earth oxides is quoted.
The elements 1-118 are now experimentally known and the studies of the chemical properties of the newest ones have begun. Up to 118Og, the PT seems well established, especially if one places the lanthanides and actinides, f0–f14 for the trivalent ions, on lines of 15 elements. These lines plug the holes left in Group 3, Periods 6-7.
For the elements 119-172, there are two proposals: 1) the long-rows proposal by Fricke et al. (1971) and 2) the short-rows proposal by Pyykkö(2011). These are based on Dirac–Slater calculations on neutral atoms, and Dirac–Fock calculations on ions, respectively. Little is still known about the chemistry of these elements and the PT is about Chemistry. A small beginning was the study of hypothetical octahedral hexafluorides, MF6, supporting the placement of E125-E129 in a 6g-series.
For heavier elements, relativistic effects must be included. Already in the 6th Period this is needed for understanding why gold is yellow, mercury is a liquid, or how the car battery works. The relativistic theory of atoms and molecules has become a vast field of nearly 19 000 publications. Its foundations at the Dirac–Fock–Breit level, including simple estimates of the Lamb shift (i.e., QED effects), appear to be under control. There are numerous reviews on the consequences of these effects in Inorganic Chemistry and their qualitative description is included in most textbooks.
What can we explain? The key message is that a large part of the chemical differences between the Periods 5 and 6 comes from relativity. Examples are Ag/Au, Cd/Hg, Sn/Pb. Most of the voltage of the lead battery comes from relativity.
Figure 1: The PT proposed by Pyykkö(2011). Modified by adding the latest names, and by emphasizing the non-monotonous cases by color. Note the nominal 5g series for Z = 121-138, starting in Group 3.
Biography
Pekka Pyykkö was born in Hinnerjoki, Finland in 1941, and received his education in the nearby city of Turku with a Ph. D. in 1967. His two latest employers were Åbo Akademi University in 1974-84, and the University of Helsinki in 1984-2009. Since November 2009 he enjoys research in Helsinki as Professor Emeritus. He now has over 330 papers. He led in 1993–98 the program 'Relativistic Effects in Heavy-Element Chemistry and Physics (REHE)' of the European Science Foundation (ESF), and in 2006-08 the Finnish Centre of Excellence in Computational Molecular Science (CMS).
Professor Donald Hilvert
Laboratory of Organic Chemistry ETH Zurich Hönggerberg HCI F 339 CH-8092 Zürich / Switzerland
Telephone: +41-44-632-3176, E-mail: hilvert@org.chem.ethz.ch,
homepage: www.protein.ethz.ch
Design, evolution and application of protein cages
Many proteins spontaneously self-assemble into regular, shell-like, polyhedral structures. Protein cage are useful—in nature and in the laboratory—as molecular containers for diverse cargo molecules, including proteins, nucleic acids, metal nanoparticles, quantum dots, and low molecular weight drugs. They can consequently serve as delivery vehicles, bioimaging agents, reaction vessels, and templates for the controlled synthesis of novel materials. Most ambitiously, self-assembly of hierarchically ordered supramolecular structures may serve as catalytic nanoreactors for short metabolic sequences. In this lecture, strategies for designing new protein containers, optimizing them by directed evolution and characterizing their structures and properties will be discussed. These efforts may provide practical routes to non-viral encapsulation systems for diverse applications in the test tube and in living cells.
Biography
Donald Hilvert is a Professor at Department of Chemistry, Swiss Federal Institute of Technology (ETH), Zurich, Switzerland. His research interests are within Enzymology, Enzyme Engineering, Molecular Evolution and Chemical Biology. He has published in total 268 articles within these fields, with coauthors from many countries. Among the most important are 1. S. Studer, D.A. Hansen, Z.L. Pianowski, P.R.E. Mittl, A. Debon, S.L. Guffy, B.S. Der, B. Kuhlman & D. Hilvert (2018). Evolution of a highly active and enantiospecific metalloenzyme from short peptides. Science 362, 1285-1288 2. T. Hayashi, M. Tinzl, T. Mori, U. Krengel, J. Proppe, J. Soetbeer, D. Klose, G. Jeschke, M. Reiher & D. Hilvert (2018). Capture and characterization of a reactive heme-carbenoid in an artificial metalloenzyme. Nat. Catal. 1, 578-584 3. N. Terasaka, Y. Azuma & D. Hilvert (2018). Laboratory evolution of virus-like nucleocapsids from non-viral protein cages. Proc. Natl. Acad. Sci. USA 115, 5432-5437. 4. D.L. Niquille, D.A. Hansen, T. Mori, D. Fercher, H. Kries & D. Hilvert (2018). Nonribosomal synthesis of backbone-modified peptides. Nature Chem. 10, 282-287. 5. R. Obexer, A. Godina, X. Garrabou, P.R.E. Mittl, D. Baker, A.D. Griffiths & D. Hilvert (2017). Emergence of a catalytic tetrad during evolution of a highly active artificial aldolase. Nature Chem. 9, 50-56. 6. Y. Azuma, R. Zschoche, M. Tinzl & D. Hilvert (2016). Quantitative packaging of active enzymes into a protein cage. Angew. Chem. Int. Ed. 55, 1531-1534 7. N. Preiswerk, T. Beck, J.D. Schulz, P. Milovníc, C. Mayer, J.B. Siegel, D. Baker & D. Hilvert (2014). Impact of scaffold rigidity on the design and evolution of an artificial Diels-Alderase. Proc. Natl. Acad. Sci. USA 111, 8013-8018. 8. R. Blomberg, H. Kries, D.M. Pinkas, P.R.E. Mittl, M.G. Grütter, H.K. Privett, S.L. Mayo & D. Hilvert (2013). Precision is essential for efficient catalysis in an evolved Kemp eliminase. Nature 503, 418-421.
Hilvert received his PhD in Organic Chemistry at Columbia University, New York, and his initial training at Eidgenössische Technische Hochschule, Zurich, Switzerland, and Rockefeller University, New York. Hilvert serves at Editor or member of editorial boards for many international journals within chemistry, medicine and biology. He has received honors and awards for his work from European, American and Asian organizations, universities and industries, The most recent are Fellow of the Royal Society of Chemistry (2004); The Emil Thomas Kaiser Award, The Protein Society (2009), Doctor of Philosophy honoris causis, Uppsala University (2011); Honorary Lifetime Membership of the Israel Chemical Society (2011); Goldene Eule & Credit Suisse Award for Best Teaching (2011); Feodor Lynen Medal, German Society for Biochemistry and Molecular Biology (2016); Biocat Award (2016); Fellow, American Academy of Arts and Sciences (2016); Moore Distinguished Scholar, Caltech (2019); Honorary Professor, Tianjin University (2019).
Professor Omar M. Yaghi
Department of Chemistry, University of California, Berkeley, California, United States
The Atom, The Molecule, The Framework
The great precision with which molecules can be examined, manipulated, and controlled is paramount in chemistry. Prof. Hassel’s contributions in deciphering the conformational dynamics of cyclohexane have had profound impact on our understanding of organic molecules and have inspired a new thinking in chemistry as a whole. An emerging area of research, we termed reticular chemistry, where organic molecules are reticulated into infinite 2D and 3D extended structures, relies heavily on the conformation of the organic linkers in directing the synthesis to a specific metal-organic framework or covalent organic framework. This presentation will show how atomic and molecular level control of conformation of organic linkers has led the emergence, development, and expansion of chemistry into the extended structure realm. In many respects, this progress is credited to the ideas regarding conformations of molecules brought forth by Hassel. We also show how these resulting structures encompass space within which molecules can be further manipulated and controlled leading to superb catalysts akin to enzymes, carbon capture and conversion to fuels, and water harvesting from desert air
Biography
Omar M. Yaghi is the James and Neeltje Tretter Chair Professor of Chemistry at University of California, Berkeley, and a Senior Faculty Scientist at Lawrence Berkeley National Laboratory. He is the Founding Director of the Berkeley Global Science Institute whose mission is to build centers of research in developing countries and provide opportunities for young scholars to discover and learn. He is also the Co-Director of the Kavli Energy NanoScience Institute focusing on the basic science of energy transformation on the molecular level, as well as the California Research Alliance by BASF supporting joint academia-industry innovations. He is known for his key scientific contributions in the discovery and development of several extensive classes of new materials: metal-organic frameworks (MOFs) and covalent organic frameworks (COFs). These materials are useful in hydrogen and methane storage, carbon capture and conversion, water harvesting from desert air, and catalysis, to mention a few. The building block approach he developed has led to an exponential growth in the creation of new materials having a diversity and multiplicity previously unknown in chemistry. He termed this field 'Reticular Chemistry' and defines it as 'stitching molecular building blocks into extended structures by strong bonds'. Among his awards are the Exxon Solid-State Chemistry Award from the American Chemical Society (1998), Sacconi Medal of the Italian Chemical Society (2004), Materials Research Society Medal (2007), Chemistry of Materials Award of the American Chemical Society (2009), Royal Society of Chemistry Centenary Prize (2010), King Faisal International Prize in Science (2015), Royal Society of Chemistry Spiers Memorial Award (2017), Albert Einstein World Award of Science (2017), BBVA Foundation Frontiers of Knowledge Award in Basic Sciences (2018), Wolf Prize in Chemistry (2018), Eni Award for Energy (2018), and Royal Swedish Academy of Sciences Gregori Aminoff Prize (2019).
Professor Tanja Kortemme
Bioengineering, the University of California, San Francisco,
e-mail: kortemme@cgl.ucsf.edu
Computational design of reprogrammed and new protein functions
There has been exciting progress in the computational design of proteins with new structures, highlighting the potential to advance many applications in biological engineering, as well as to provide insights into the design principles of natural protein functions. Many significant challenges remain, both in the accuracy of current computational approaches, and in the complexity of protein geometries and functions that can be designed at present. I will discuss our recent progress with computational methods and describe new approaches and their applications. Our new work includes (i) reshaping of proteins for reprogrammed functions using principles from the field of robotics, (ii) creating small molecule binding sites entirely de novo to detect and respond to new molecular signals in living cells, and (iii) controlling protein shapes to create protein fold families for new functions.
Biography
Tanja Kortemme is a Professor of Bioengineering at the University of California, San Francisco. She received her Ph.D. from the European Molecular Biology Laboratory in Heidelberg, Germany, and was an EMBO and Human Frontier Science Program postdoctoral fellow at the University of Washington, Seattle. Her laboratory’s scientific contributions include foundational methods for computational protein design and their application to engineer biological structures and functions not existing in nature, such as the first computationally designed new protein-protein interfaces, signaling proteins with new specificities, and de novo engineered binding sites recognizing and responding to new small molecule signals. A more recent research focus uses systematic molecular perturbations to map and control cellular behavior. Her honors include an Alfred P. Sloan Fellowship, a CAREER award from the National Science Foundation, and a W.M. Keck Foundation Research Award. She was recently selected as a Chan-Zuckerberg Biohub investigator.
Professor Richard Henderson
MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus
Cambridge CB2 0QH, U.K., tel: +44-(0)1223-267065, web: http://www2.mrc-lmb.cam.ac.uk/groups/rh15/, e-mail: rh15@mrc-lmb.cam.ac.uk
Electron cryomicroscopy to investigate the chemistry of life
In the last few years, single particle electron cryomicroscopy (cryoEM) has experienced a quantum leap in its capability, due to improved electron microscopes, better detectors and better software, and this is revolutionising structural biology. Using the plunge-freeze technique invented by Jacques Dubochet and his colleagues, a thin film containing a suspension of the macromolecules of interest is plunged into liquid ethane at liquid nitrogen temperature, creating a frozen film of amorphous ice in which individual images of the structures can be seen in many different orientations. Subsequent computer-based image analysis is then used to determine the three-dimensional structure, frequently at near-atomic resolution. This method has been incredibly successful during the last 6 years, so that many biological structures that were previously intractable have now been revealed. I will show some topical examples and discuss how further technical improvements might be made.
Biography
Richard Henderson is a structural biologist, with a background in physics from Edinburgh University. After a Ph.D. at the Medical Research Council Laboratory of Molecular Biology (MRC-LMB) working on enzyme mechanisms, he developed an interest in membrane proteins as a postdoc at Yale. After returning to the MRC-LMB, he collaborated with Nigel Unwin to use electron microscopy to determine the structure of bacteriorhodopsin in two-dimensional crystals, first at low resolution and later at atomic resolution. With Chris Tate, he helped to develop a method named “conformational thermostabilisation” that allows any membrane protein to be made more stable while at the same time retaining a chosen conformation of interest. This helped the crystallization and structure determination of several G protein–coupled receptors (GPCRs), and has also been useful for cryoEM. Most recently, he has been working to improve the cryoEM methodology.
Associated Professor Odile Eisenstein
Dep of Chemistry, University of Oslo