Special Lectures
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Martin Rees
UK
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Martin Rees is President of the Royal Society and also Master of Trinity College, and Professor of Cosmology and Astrophysics at the University of Cambridge. He is also Visiting Professor at Leicester University and Imperial College London. He was appointed Astronomer Royal in 1995. His main research interests are in cosmology, the formation of galaxies, and in 'high energy astrophysics' -- in particular, in 'extreme' cosmic phenomena which offer insights into physics complementary to what can be learnt by laboratory experiments. He has received numerous awards for his work, including the Balzan and the Crafoord Prize, and is a member of several foreign academies. In addition to his research, he has written several general books and many articles on science and public policy. He was nominated to the UK's House of Lords in 2005.
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Monday 31 August, 18:15 - 19:30 - Auditorium
Title & synopsis
From 'Big Bang' to biosphere: a cosmic perspective
Darwin concluded "The Origin of Species" with these famous words: "whilst this planet has gone cycling on according to the fixed law of gravity, from so simple a beginning forms most wonderful and most beautiful have been and are being evolved". Astronomers aim to trace cosmic history back before Darwin's "simple" beginning: to understand the origin of planets, stars and atoms. The lecture will summarise current ideas on how complex structures emerged from an amorphous 'big bang'.
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Kenneth C Holmes
DE
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Kenneth C Holmes obtained his B.A. at St. Johns College, Cambridge. He obtained his Ph.D. in 1959 at Birkbeck College London working on the structure of tobacco mosaic virus with Rosalind Franklin. Franklin died during this period and the work was completed with Aaron Klug. After a post-doc (1960-61) at Childrens' Hospital Boston, where he started to work on muscle structure with Carolyn Cohen, he returned to the newly opened Laboratory of Molecular Biology in Cambridge. Here he developed methods and X-ray optics for the analysis of structures by X-ray fibre diffraction. He worked with Aaron Klug on the structure of tobacco mosaic virus and with Hugh Huxley on muscle. In 1968 he moved to Heidelberg to open the Department of Biophysics at the Max Planck Institute for Medical Research where he remained as director until his retirement in 2003. During this time he completed the structure of tobacco mosaic virus and solved the structures of a number of protein molecules by protein crystallography including the structure of the muscle protein actin. He solved the structure of the actin filament using X-ray fibre diffraction data in combination with crystal data. Increasingly he has worked on the molecular mechanism of muscle contraction. In 1970 he pioneered the use of synchrotron radiation as a source for X-ray diffraction and founded the EMBL outstation at DESY Hamburg. He was elected to the Royal Society in 1981 and is a member of a number of Scientific Academies.
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Saturday 29 August, 18:30 - 19:15 - Auditorium
Title & synopsis
Fifty years of protein structure
In 1934 J.D. Bernal and Dorothy Crowfoot showed that crystals of pepsin diffracted X-rays very well, thus demonstrating that proteins have defined structures and that all molecules of a particular protein are identical in form. Later Bernal’s student Max Perutz started to solve the structure of crystalline hemoglobin from the X-ray diffraction data. However, this took another 25 years. The main hold up was dealing with the ‘phase problem’. Diffraction from a crystal in an X-ray beam comes out in well-defined directions called ‘reflections’. On X-ray film this gives sets of spots of varying intensity. Rotating the crystal gives the diffraction from all possible views of the crystal. A Fourier Transform of this data yields an electron density map of the crystal. However, the relative time of arrival of the wave-front of each reflection (the phase) at the detector is lost. Unfortunately, this is essential information. Perutz found that phase could be recovered experimentally by adding heavy atom markers to the protein. John Kendrew, a colleague of Perutz, was then able to use this method to obtain the atomic structure of myoglobin, a smaller relative of hemoglobin. The structure was published in Nature 50 years ago. This epoch-making result demonstrated that, by application of X-ray crystallography to proteins, it would be possible to understand most biological function in chemical terms, which was Bernal’s vision. In 1962 Kendrew and Perutz shared the Noble Prize for Chemistry. Initially the method was heroic and remained esoteric. However, technical advances such as cloning and expressing proteins in bacteria, intense synchrotron X-ray sources and automation have now transformed the method into a freely available technique. There are now over 100,000 protein structures in the database. Moreover, the method has been applied to ever-larger complexes such as intact viruses and whole ribosomes so that it is now an essential technique and a pillar of molecular biology. |
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Harald zur Hausen
DE
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Harald zur Hausen studied Medicine in Bonn, Hamburg and Düsseldorf and received his M.D. in 1960. After his medical internship he worked as postdoc Düsseldorf and as Assistant Professor at the Children’s Hospital, Philadelphia. In 1969 he was employed as “Privat-Dozent”, Institute of Virology, Würzburg. 1972 he was appointed as Professor and Chairman of the Institute of Clinical Virology in Würzburg, since 1977 in a similar position in Freiburg, Germany. Between 1983 and 2003 he was Scientific Director, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg. Since May 2003 he is Professor emeritus. He received a larger number of scientific awards, in 2008 the Nobel Prize for Physiology or Medicine. He holds seven honorary doctorates. He is elected member of several scientific academies and organizations, among them Institute of Medicine, US National Academy of Sciences, European Molecular Biology Organization (EMBO), and German National Academy Leopoldina. He is author or co-author of more than 275 publications.
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Saturday 29 August, 19:15 - 20:15 - Auditorium
Title & synopsis
Infections & human cancers: facts & perspectives
Presently approximately 21% of the global cancer incidence can be linked to viral, bacterial or parasitic infections. Thus, infections can be considered as the second most important identified risk factor for human cancers; smoking still remains the first. The mechanisms by which the various infections contribute to cancer development differ substantially. In DNA virus infections frequently viral oncogenes are inserted into cancer cells. Their function represents an essential requirement for induction of the respective cancer and for the maintenance of the malignant phenotype. They are therefore considered as direct carcinogens. Other agents act indirectly by inducing immunosuppression, resulting in activation of additional latent tumorviruses or by inducing long-lasting chronic inflammatory processes. Although many of these infections appear to represent mandatory factors for the respective cancer induction, in each case genetic modifications within the respective host cell are additional requirements. The identification of infectious agents causing human cancers led to important medical consequences. Prevention of two wide-spread human cancers (cervical cancer and Hepatitis B virus-linked liver cancer) by vaccination is now achievable. Elimination of Helicobacter pylori by antibiotics and of schistosoma infection by chemotherapy also contribute to cancer prevention. In addition, knowledge of causative factors facilitates early diagnosis of these cancers. There exist epidemiological hints that additional human cancers might be linked to infectious events. This accounts in particular for childhood leukemias, Epstein-Barr virus-negative Hodgkin's disease, some basal cell carcinomas of the skin and human cancers otherwise linked to nutritional factors. The available evidence will be summarised.
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Svante Pääbo
DE
Max-Planck Institute for Evolutionary Anthropology,
DE
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Dr. Svante Pääbo studies the genetic underpinnings of human evolution. He has developed technical approaches as well as criteria to authenticate results that have allowed DNA sequences from extinct creatures such as mammoths, ground sloths and Neanderthals to be determined. He is currently directs the efforts to sequence the entire Neandertal genome. He also works on the comparative genomics of humans and apes, particularly the evolution of gene activity and genetic changes that may underlie aspects of traits specific to humans such as speech and language. He is currently a Director at the Max-Planck Institute for Evolutionary Anthropology in Leipzig, Germany.
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Incorporated into the Plenary Lecture: Chromosomes: dynamics, maintenance & evolution; Sunday 30 August, 12:00 - 12:45 - Auditorium
Title & synopsis
A Neandertal perspective on human origins
Neandertals, who became extinct around 30,000 years ago, are the closest relatives of extant humans. We are currently sequencing the Neandertal genome and analyze it together with several colleagues in Croatia, Spain, Germany and the US. To date, we have recently determined the sequences of more than 1.1 billion DNA fragments extracted from Neandertal fossils from Vindija Cave in Croatia. I will discuss the nature and location of chemical damage in the ancient DNA molecules and how it causes errors in the DNA sequences. I will also describe methods we have developed to prevent and detect contamination of the bones and experiments with DNA from modern human. By using novel computer algorithms that take several features of ancient DNA into account we have identified almost 3.7 billion bases from across the Neandertal genome. This allows over 60% of all nucleotide sequences in the genome to be studied and shows that Neandertal DNA sequences diverged from human sequences on average ~830,000 years ago. Using these sequences we can now for the first time be determined which of the substitutions that occurred on the human evolutionary lineage happened after fully modern humans diverged from the Neandertal-modern human ancestor. The Neandertal genome, which falls partially within the coalescence of human genes, also allows novel approaches to detect positive selection in modern humans.
We have furthermore sequenced several entire Neandertal mitochondrial genomes from three archaeological sites in Europe. This allows us to begin to reconstruct the population history of Neandertals.
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Fotis Kafatos
UK
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Fotis C. Kafatos is currently Professor of Immunogenomics at Imperial College London, and President or the European Research Council. He was previously Director-General of the European Molecular Biology Laboratory (EMBL, 1993-2005) and Professor at Harvard (1969-1994). He founded and directed the Institute of Molecular Biology and Biotechnology at the Research Centre of Crete from 1982 to 1993. His current scientific work is on malaria research with emphasis on mosquito genomics and immunity of Anopheles to the Plasmodium parasite. He is a Foreign Member of the Royal Society of London, the French Academy of Sciences and Member of the US National Academy of Sciences, the
American Academy of Arts and Sciences, the Pontifical Academy of Sciences, EMBO and Academia Europaea.
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Monday 31 August, 13:30 - 15:30 - Room C-D
Title & synopsis
The European Research Council takes flight
The European Research Council (ERC) is an independent agency funding frontier research in all disciplines, from the humanities to engineering, across Europe. Kafatos reports and analyses the results from the first two ERC calls, the latest developments and the challenges that face this Research Council, the cutting edge of Europe’s aspiration to become the most dynamic and competitive knowledge-based society in the world.
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