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	Ferid Murad born September 14, 1936 in Whiting, Indiana, USA Address: Department of Integrative Biology, Pharmacology and Physiology, University of Texas Medical School at Houston, P.O. Box 20708, Houston, TX 77225, USA Academic Education 1958-65 M.D., Western Reserve University, School of Medicine, Cleveland, OH 1958-65 Ph.D., Department of Pharmacology, Western Reserve University, School of Medicine, Cleveland, OH Appointments and Professional Activities 1975-81 Professor, Depts of Internal Medicine and Pharmacology, Univ of Virginia School of Medicine, Charlottesvill 1971-81 Director, Clinical Research Center, Univ of Virginia, Charlottesville, VA 1973-81 Director, Division of Clinical Pharmacology, Dept of Internal Medicine, Charlottesville, VA 1981-89 Professor, Departments of Internal Medicine and Pharmacology, Stanford Univ, Stanford, CA 1981-86 Chief of Medicine, Palo Alto Veterans Administration Medical Center, CA 1988- Professor (Adjunct), Department of Pharmacology, Northwestern Univ Medical School, Chicago, Illinois 1990-92 Vice President, Pharmaceutical Research & Development, and Corporate Officer, Abbott Laoratories, Abbott Park, Illinois 1993-95 CEO/President, Molecular Geriatrics Corporation, Lake Bluff, Illinois Fellowships and Awards Ciba Award Recipient, 1988 Albert Lasker Basic Medical Research Award, 1996 The Nobel Assembly at the Karolinska Institute

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	Robert Huber was born February 20, 1937 in Munch, Germany. In 1956, he graduated from the Humanistische Karls-Gymnasium. He began studying chemistry at the Technische Hochschule (later Technische Universität) in Munch from which he received the Diploma in Chemistry in 1960. In 1963, he received a Dr. rer. nat researching the crystal structure of a diazo compound. He continued crystallographic studies at the University and the Physiologisch-Chemisches Institut der Universität München. In 1971, the University of Basel offered him a chair of structural biology at the Biozentrum and the Max-Planck-Gesellschaft the position of a director at the Max-Planck-Institut für Biochemie where he stayed until 2005. In 2005, he was made Director Emeritus. He also continued with the Technische Universität München, where he became Professor in 1976.

In 1967, he began crystallographic work on the insect protein erythrocruorin. The elucidation of this structure and its resemblance to the mammalian globins as determined by Perutz and Kendrew in their classical studies suggested for the first time a universal globin fold of the insect metamorphosis hormone ecdysone. In 1970, he started research on the pancreatic trypsin inhibitor, proteolytic enzymes and their natural inhibitors, proteases, their proenzymes, and complexes between them. He also studied the structure of immunoglobulin, the first glycoprotein to be analyzed in atomic detail. He elucidated the structure and the chemical nature of the selenium moiety in glutathione peroxidase and the structures of citrate synthase in different states of ligation and a very large multienzyme complex, heavy riboflavin synthase. Studies of proteins involved in excitation energy and electron transfer, lightharvesting proteins led to the structure of the reaction center.

For the determination of the three-dimensional structure of a photosynthetic reaction centre, he shared the Nobel Prize in Chemistry with Johann Deisenhofer and Hartmut Michel in 1988. He received the E. K. Frey Medal from the German Society for Surgery in 1972, the Otto Warburg Medal from the German Society for Biological Chemistry in 1977, the Emil von Behring Medal from the University of Marburg in 1982, the Keilin Medal from the London Biochemical Society and the Richard Kuhn Medal from the Society of German Chemists, 1987, and the Sir Hans Krebs Medal in 1992. He has also received numerous honorary doctorates and memberships in foreign chemical and biochemical societies.

He married Christa Essig in 1960 and they have four children.

References:

http://www.bookrags.com/biography/robert-huber-wob/

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	Prof. Edmond Fischer (born 1920), is a Shanghai-born Swiss biochemist. He completed his PhD in chemistry during World War II at the University of Geneva (Switzerland was officially neutral during the war). After completing his PhD, he went to the United States, to conduct postdoctoral work. He had originally planned at working in Caltech but instead changed to the University of Washington, Seattle because it reminded him and his wife of Switzerland. There he met his eventual collaborator Edwin Krebs. Fischer joined the department of physiology at the University of Washington, Seattle. Physiology is the study of the normal functions of the body and the various organs.

Physiology research in the past focused on observing a physiological response followed by trying to identify the reason for it, research today isolates genes and proteins and then tries to identify what they do. Many important physiological responses were found to be controlled by hormones from the endocrine glands.

Both Fischer and Krebs were then post-doctoral fellows (i.e. they did not have their own lab) in the Carl and Gerty Cori lab. The Cori’s were prominent world leaders in endocrinology.. Edwin Krebs was hesitant, as he later remarked in an interview, “the fact that I had been in Cori’s lab… at that time, post-docs when they left the lab did not work on the problem that was going on in their previous lab.” He decided to work on it, after rationalising that five years out of Cori’s lab would have blurred that non-crossable line.

Even with a larger question in mind, progress requires small and steady steps to a goal. Krebs and Fischer decided to focus on the problem of phosphorylase activation-inactivation. Phosphorylation is the process of adding a phosphate group a protein or other organic molecule. This process serves as a switch to turn on/off a particular protein activity.

They honed in on the enzyme glycogen phosphorylase. Glycogen degradation is important because it is what produced blood glucose in the liver and Adenosine Triphosphate (ATP), the energy currency that all living things need to survive. Phosphorylase was known then to be under complex hormonal control. At the resting state, phosphorylase is inactive, when conversion is required for various purposes, the enzyme is instantly activated by hormones such as insulin or adrenalin. However, after a meal when there was a lot of glycogen phosphorylase was inactivated. What was clear was that phosphorylase was pivotal in this cycle.

The work was not something entirely new. Early in the 1930s, husband and wife team Carl and Gerty Cori had discovered that the first step of glycogen degradation was catalysed by phosphorylase. The Cori Lab had isolated both the active and inactive form of phosphorylase and assumed that a product Adenosine Monophosphate (AMP) was the key in the reversal of the process. Their experiments failed, they could not find AMP. Instead of carrying on, they dropped the project and did other work. The Cori’s would go on to win the Nobel Prize for their other work for their discovery of the Cori Cycle.

The Cori method for obtaining phosphorylase was rather ancient even by 1950s standards – they use simple filter paper. Krebs and Fischer decided that they would be more modern and use centrifugation. Somehow, they could never obtain the active phosphorylase. Frustrated, they decided to revert to Cori’s method. The results would stun them.

After passing through the filter paper, the initially inactive phosphorylase was activated. For the two ambitious young men, that was a massive disappointment – they had thought that they would discover some complex system instead of simple filter paper. They refused to accept that the inactive phosphorylase was what it was, writing in their logbooks “false” phosphorylase B instead. It was only later, that they discovered that the filter paper then had minute amounts of Calcium ions (Ca2+), which was sufficient to convert inactive B form phosphorylase into active A form phosphorylase with the use of ATP. ATP degraded very quickly, however.

The two young men had no access to ATP, what they had though were friends.

Arthur Kornberg (who would go on to win the Nobel Prize for Physiology or Medicine in 1959) was then working in the University of Washington in St Louis, Missouri. He had ATP to spare. They then asked their friend to send them some.

Kronberg sent them some ATP samples and they managed to prove that inactive phosphorylase was converted into an active form by a phosphorylase kinase, Magnesium ion, ATP and Ca2+; and the active form was made inactive by a phosphorylase phosphatase. They shot a paper off to the Journal of Cell Biology and were fortunate to have in them Cori who was as excited as they were.

The system became even more complicated the more they studied it. They soon realised that the system was not linear but a cascade of kinases. It was at the same time that Earl Sutherland and his group reached the same conclusion. Sutherland discovered cyclicAMP as a mediator for hormones that conventional wisdom was turned on its head. However he had no idea what it could do. After hours of talking and drinking they convinced Sutherland to send them samples of cyclicAMP, enabling the eventual discovery of hormonal control of glycogenolysis.

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	Jean-Marie Lehn Born on September 30, 1939 at Rosheim, Bas-Rhin Addresses ISIS, Université Louis Pasteur 8 allée Gaspard Monge, BP 70028, F-67083 Strasbourg cedex Tel. +33-390-245-145 Fax +33-390-245-140 E-mail lehn@isis.u-strasbg.fr Collège de France 11 place Marcelin Berthelot, F-75005 Paris Tel. +33-144-271-360 Fax +33-144-271-356

Director Laboratoire de Chimie Supramoléculaire
ISIS, Université Louis Pasteur, Strasbourg

Laboratoire de Chimie des Interactions Moléculaires, Collège de France, Paris

Director at the Nanotechnologie Institute of the Research Center of Karlsruhe, since 1998

EducationUndergraduate Studies, University of Strasbourg: Licence ès-Sciences (Bachelor of Sciences), Strasbourg, 1960 Graduate work on "Conformational Studies of Triperpenes"; with Professor Guy Ourisson, University of Strasbourg Doctorat-ès-Sciences (Ph.D.), University of Strasbourg, 1963 Post-Doctoral Research Fellow at Harvard University, 1964: work on vitamin B12 total synthesis with Professor Robert B. Woodward

Appointments
Member of the Centre National de la Recherche Scientifique (CNRS), 1960-66
Maître de Conférences (Assistant Professor) at the University of Strasbourg, 1966-69
Professeur sans chaire (Associate Professor) at the University Louis Pasteur of Strasbourg, 1970
Professor of Chemistry at the University Louis Pasteur of Strasbourg, 1970-1979
Professor at Collège de France, Paris, since October 23rd 1979; Chair of Chimie des Interactions Moléculaires
Visiting Professor of Chemistry at Harvard University, 1972 (Spring), 1974 (Spring), and on a part time basis until 1980
Visiting Professor of Chemistry at the E.T.H. Zürich, 1977
Alexander Todd Visiting Professor of Chemistry, Cambridge University, 1984
Visiting Professor, University of Barcelona, 1985
Rolf-Sammet Gastprofessor, Frankfurt University, 1985-86
Heinrich-Hertz Gastprofessor, Karlsruhe University, Nov., Dec. 1989
Robert Burns Woodward Visiting Professor, Harvard University, 1997, 2000
Newton Abraham Professor, Lincoln College, Oxford University, 1999-2000
Adjunct Professor at the Asian Institute of Technology, Bangkok, 2005

Honorary Degrees
Honoris Causa Doctorates
Hebrew University of Jerusalem, 1984
Universidad Autonoma, Madrid, 1985
Georg-August University of Göttingen, 1987
Université Libre of Bruxelles, 1987
Iraklion University, 1989
Università degli Studi di Bologna, 1989
Charles University of Prague, 1990
University of Sheffield, 1991
University of Twente, 1991
University of Athens 1992
Polytechnical University of Athens, 1992
Illinois Wesleyan University, 1995
Université de Montréal, 1995
University of Bielefeld, 1998
Honorary Professor, University of Science and Technology of China, Hefei, 1998
Honorary Professor, Southeast University, Nanjing, 1998
Weizmann Institute of Science, Rehovot; 1998
Faculté des Sciences Appliquées, Université Libre de Bruxelles, 1999
Nagoya University, 2000
Université de Sherbrooke, 2000
Università di Trieste, 2001
Honorary Professor, Shanghai Jiao Tong University, 2003
Honorary Professor, Nanjing University, 2003
Royal Institute of Technology, Stockholm, 2003
University of St. Andrews, 2004
Heriot Watt University, Edinburgh, 2005
Technical University, St Petersburg, 2005
Mazaryk University, Brno, 2005
Honorary Professor, Beijing University, 2005
Kyushu University, 2005

Awards
Bronze Medal of the CNRS, 1963
Adrian Prize of the Société Chimique de France, 1968
Silver Medal of the CNRS, 1972
Raymond Berr Prize of the Société Chimique de France, 1978
Gold Medal of the Académie Pontificale des Sciences, 1981
Gold Medal of the CNRS, 1981
Pierre Bruylants Medal, Louvain, 1981
Paracelsus Prize of the Swiss Chemical Society, 1982
Alexander von Humboldt Forschungspreis, 1983
Prize of the Commissariat à l'Energie Atomique awarded by the Académie des Sciences, 1984
Rolf-Sammet Prize, Frankfurt University, 1985
Prize of the Fondation Alsace, 1986
George Kenner Prize, University of Liverpool, 1987
Nobel Prize in Chemistry, 1987
Sigillum Magnum, University of Bologna, 1988
Minnie Rosen Award, 1989
Vermeil Medal of the Ville de Paris, 1989
Gold Medal of the Société d'Encouragement au Progrès, 1989
Karl-Ziegler Prize, Gesellschaft Deutscher Chemiker, 1989
Grand Bretzel d’Or, Institut des Arts et Traditions Populaires d’Alsace, 1992
Bonner Chemiepreis, 1993
1992 "Ettore Majorana-Erice-Science for Peace" Prize, 1994
Gold Medal of the Société Académique Arts–Sciences–Lettres, 1995
Gold Medal of Comenius University, Bratislava, 1995
Golden Memorial Medal of the Faculty of Sciences, Charles University, Prague, 1995
Honorary Medal of the Institute of Physical Chemistry, Polish Academy of Sciences, Warszawa, 1996
The Davy Medal of the Royal Society, 1997
Lavoisier Medal 1997 of the Société Française de Chimie
Top 75 Award, C&N, American Chemical Society, 1998
Allan R. Day Award of the Philadelphia Organic Chemists' Club, 1998
1998 Messel Medal, Society of Chemical Industry, London
Premio Barocco, 2003
Gold Medal "Giulio Natta" of the Italian Chemical Society, 2003
JSPS Award (Japan Society for the Promotion of Science), 2003
Gold Medal of the 70th Anniversary of the Fondation de la Maison de la Chimie, 2004
Gold Medal of the University Paul Sabatier Toulouse III, 2005

Memberships
Foreign Associate of the National Academy of Sciences of the USA, 1980
Foreign Honorary Member of the American Academy of Arts and Sciences, 1980
Foreign Member of the Royal Netherlands Academy of Arts and Sciences, 1983
Member of the Académie des Sciences, Institut de France, 1985
Foreign Member of the Deutsche Akademie der Naturforscher Leopoldina, 1985
Foreign Member of the Accademia Nazionale dei Lincei, 1985
Honorary Member of the Union des Physiciens, 1986
Foreign Member of the American Philosophical Society, 1987
Honorary Member of the Académie Européenne des Sciences, des Arts et des Lettres, 1987
Honorary Member of the Royal Society of Chemistry (Belgium), 1987
Honorary Fellow ot the Royal Society of Chemistry (Great-Britain), 1987
Member of the Academia Europaea, 1988
Member of the Académie d'Alsace, 1989
Honorary Fellow of Fondation de la Maison de la Chimie, 1989
Foreign Associate of the Akademie der Wissenschaften und der Literatur-Mainz, 1989
Honorary Member of the Yugoslav Academy of Sciences and Arts, 1990
Member of the Akademie der Wissenschaften of Göttingen, 1990
Associate Member of the Koninklijke Vlaamse Academie van België voor Wetenschappen en Kunsten, 1990
Honorary Fellow of the Indian Academy of Sciences, 1991
Foreign Member of the Polish Academy of Sciences, 1991
Foreign Associate of the Academy of Arts and Sciences of Puerto Rico, 1991
Foreign Member of the Ukrainian Academy of Sciences, 1992
Honorary Member, Institut Grand Ducal, Luxembourg, 1992
Foreign Member of the Royal Society, 1993
Honorary Member of the Romanian Academy, 1993
Honorary Foreign Member of the Korean Academy of Science and Technology (KAST), 1995
Member of the Pontifical Academy of Sciences, 1996
Foreign Member of the Third World Academy of Sciences, 1996
Honorary Member of the Czech Learned Society, 1997
Honorary Member of the Gesellschaft Deutscher Chemiker, 1997
Foreign Member of the Academy of Sciences of Turin, 1999
Honorary Member of the Royal Irish Academy, Section Science, 1999
Foreign Member of the Russian Academy of Sciences, 1999
Honorary Fellow of the Institute of Physics, 1999
Member of the Académie des Technologies, Institut de France, 2001
Honorary Member of the Hungarian Academy of Sciences, 2001
Honorary Member of the Hungarian Academy of Sciences, 2001
Honorary Fellow of the Singapore Institute of Chemistry, 2001
Member of the International Academy of Humanism, 2001
Honorary Member of The Chemical Society of Japan (CSJ), 2002
Honorary Fellow of the Chemical Research Society of India, 2002
Consulting Honorary Member of The World Innovation Foundation, 2003
Corresponding Member of the Slovenian Academy of Sciences and Arts, 2003
AAAS Fellow, American Association for the Advancement of Science, 2003
Honorary Fellowship of IChemE Institution of Chemical Engineers, 2003
President of the Academia Bibliotheca Alexandrinae, 2004
Foreign Member of the Chinese Academy of Sciences, 2004
Member of the Gesellschaft Österreichischer Chemiker, 2004
Honorary Member of the Académie des Sciences Inscriptions et Belles Lettres de Toulouse, 2005
Honorary Member of the Real Academia Sevillana de Ciencias, 2005
Honorary Member of the Société Française de Chimie, 2005

Decorations
Chevalier dans l'Ordre National du Mérite, 1976
Chevalier de l'ordre de la Légion d'Honneur, 1983
Officier de l'ordre de la Légion d'Honneur, 1988
Chevalier dans l'Ordre des Palmes Académiques, 1989
Member of the Order "Pour le Mérite" für Wissenschaften und Künste (RFA), 1990
Officier dans l'Ordre National du Mérite, 1993
Commandeur de l'Ordre de la Légion d'Honneur, 1996
Ostereischiches Ehrenkreuz für Wissenschaft und Kunst, Erste Klasse, 2001
Grand Officer of the Order of Cultural Merit of Romania, 2004

Scientific Work
790 publications; 3 books
"Chemia Supramolekularna",
Collection of publications by J.-M. Lehn, organised and translated into Polish under the direction of Janusz Lipkowski, Institute of Physical
Chemistry, Polish Academy of Sciences, 1985.
B. Dietrich, P. Viout, J.-M. Lehn,
"Aspects de la chimie des composés macrocycliques",
InterEditions/Editions du CNRS, 1991.
"Macrocyclic Chemistry – Aspects of Organic and Inorganic Supramolecular Chemistry",
VCH, Weinheim, 1993. J.-M. Lehn, "Supramolecular Chemistry – Concepts and Perspectives",
VCH, 1995. "La chimie supramoléculaire : Concepts et perspectives",
Traduit de l’anglais par A. Pousse, De Boeck Université, Bruxelles, 1997.
- Japanese Version, translated by Y. Takeuchi, Kagaku Dojin, Tokyo, 1997.
- Russian Version, translated by E.V. Boldyreva; coeditors, V.V. Vlassov and A.A. Varnek; Nauka, Novosibirsk, 1998.
- Chinese Version, translated by X. Shen, Peking University, Beijing, 2002.

Fields of Research
Theoretical Organic Chemistry: Ab initio conformational analysis: computation of nitrogen and phosphine inversion, of the electronic structure of hydrocarbons, of stereoelectronic effects on chemical reactivity; theoretical studies of molecular receptors and recognition processes. Dynamic Nuclear Magnetic Resonance: Studies of conformational rate processes, internal rotation and nitrogen inversion. Molecular Dynamics and Liquid Structure from Nuclear Magnetic Relaxation data. Nuclear Quadrupole Resonance. Supramolecular Chemistry: Cryptates: Design, synthesis and properties of ligands forming stable and selective inclusion complexes with metal ions; di- and poly-nuclear cryptates; bioinorganic models; photoactive and electroactive cryptates; cluster cryptates; energy and electron transfer processes. Molecular Recognition, Molecular Receptors and Coreceptors: Design, synthesis and properties of macropolycyclic complexing agents binding selectively one or several molecular substrates: metalloreceptors; photoactive receptors; cyclointercalands. Anion Coordination Chemistry: Anion cryptates; receptors and coreceptors for anionic substrates; selective complexation of organic, inorganic and biological anions. Supramolecular Catalysis: Design and properties of molecular catalysts performing a reaction on bound substrate species; enzyme models; cocatalysis. Transport Processes: Design of selective carriers; transport of anions, cations and molecules; thermodynamic and kinetic properties; transport regulation; coupling to chemical potentials (protons, electrons) and to light. Selfassembly and Selforganisation: Design of systems generating given supramolecular architectures by molecular recognition directed spontaneous assembly of the components; programmed chemical systems; hydrogen bonding and coordination interactions; selforganisation of organic and inorganic entities; polymolecular assemblies. Supramolecular Materials: Recognition materials, supramolecular polymers, liquid crystals, vesicles, inorganic materials. Chemionics: Molecular Photonic, Electronic and Ionic Devices: Photoactive and electroactive cryptates; energy and electron transfer processes; light conversion; photo-antenna; ion transfer; molecular and ionic switching and amplifying processes; molecular protonics. Semiochemistry: Generation and processing of optical, electronic and ionic chemical signals; ion detection; ion pulses; non-linear optical properties. Photochemistry and Solar Energy Storage: Photochemical activation of small molecules by means of transition metal complexes; photogeneration of hydrogen and oxygen; water photolysis; photoreduction of CO2; design of photoinduced charge separation systems. Structural and Dynamic Studies by Multinuclear NMR on supramolecular complexes (in collaboration with the NMR Laboratory). Bioorganic Chemistry and Biological Applications: Models of biological receptors, of enzymes and of biological transport processes; immunological labelling agents, selective nucleic acid reagents, helical and metallo-nucleic complexes; artificial gene transfer vectors. Dynamic Combinatorial Chemistry: Design of virtual combinatorial libraries; application to biological targets and to materials.

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	Hartmut Michel was born in Ludwigsburg, Württemberg, in the southwestern part of the Federal Republic of Germany on July 18, 1948, as the elder son of Karl and Frieda Michel. My ancestors lived in that area for generations, mainly as farmers. There the inherited land is equally divided among sisters and brothers, and not enough land was left for one family's living during my grandparents' generation. During the day my father worked in a factory as a joiner, my mother at home as a dressmaker, in the evenings and on Saturdays care had to be taken of the huge gardens.

As a child I liked to play outside, to stroll through the fields, and I was an active member of the local children's gang, frequently being chased by field guards and building supervisors. Nevertheless, my performance at school was very good, and mainly due to the influence of my mother I was allowed to attend high school. At age eleven I became a member of the circulating library of my home town. From there on I was rarely seen outside, but was reading two to four books per week, the subjects ranging from archaeology over ethnology and geography to zoology. Needless to say that I did not do much homework. At school my favorite subjects were history, biology, chemistry and physics. Especially the teaching in physics was excellent. Most of my understanding of it I got at high school, not at the university.

In parallel, my interest in molecular biology rose. In 1969 - after the obligatory military service - I applied to study biochemistry at the University of Tübingen. At that time Tübingen was the only place in Germany, where one could study biochemistry from the first year, and I was happy to be accepted. Studying biochemistry meant that one had to take part in nearly the same amount of lectures and courses as chemistry students in addition to numerous lectures and courses in biology. The atmosphere between senior teachers and students was impersonal, and the only time I talked to the full professor of biochemistry was during the final examination. However, the possibility existed to work for one year in the various biochemistry labs at the University of Munich and the Max-Planck-Institut für Biochemie instead of attending lab courses in Tübingen. I took that chance in 1972/1973, and at the end I was convinced that academic research was what I wanted to do.

After the examination in Tübingen in 1974 I did the experimental part of my biochemistry diploma in Dieter Oesterhelt's lab at the Friedrich Miescher-Laboratorium of the Max-Planck-Gesellschaft in Tübingen. In cooperation with Walter Stockenius, Dieter Oesterhelt had discovered bacteriorhodopsin in halobacteria and later proposed that it acts as a lightdriven proton pump in the framework of Peter Mitchell's chemiosmotic theory. During my diploma work I characterized the ATPase-activity of halobacteria. In 1975, Dieter Oesterhelt moved to Würzburg. I joined him, and as a thesis I correlated the intracellular levels of adenosine di- and triphosphate with the electrochemical proton gradient across the halobacterial cell membrane. Having received the doctorate in June 1977 I tried to fuse delipidated bacteriorhodopsin with bacterial vesicles in order to achieve light-driven amino acid uptake. Upon storage in the freezer the delipidated bacteriorhodopsin yielded solid, glass-like aggregates. On the basis of this observation I was convinced that it should be possible to crystallize membrane proteins like bacteriorhodopsin, which was considered to be impossible at that time. With Oesterhelt's help I started the experiments, and already four weeks later we obtained a new two-dimensional membrane crystal of bacteriorhodopsin. It was not the three-dimensional crystal we wanted, but allowed me to travel to the MRC at Cambridge, England, and to do electron microscopical studies together with Richard Henderson. Back in Würzburg, we observed the first real three-dimensional crystals of bacteriorhodopsin in April 1979. The success led me to cancel my plans to do post-doctoral studies with Susumu Ohno, Duarte, California, on sexual differentiation in mammals. Instead of this, I moved with Dieter Oesterhelt again, this time to the Max-Planck-Institut für Biochemie at Martinsried near Munich, where he became a department head and director. Before moving to Munich, Ilona Leger became my wife. Her understanding and patience helped me a lot.

A promising aspect of the move to Martinsried was the possibility of a cooperation with Robert Huber and colleagues, who at the Max-PlanckInstitut had established a very productive department for X-ray crystallographic protein structure analysis. Our bacteriorhodopsin crystals were found to diffract X-rays, but to be too small and too disordered for a structural analysis. We tried to improve size and quality of the crystals. Since all the X-ray crystallographers had beautifully diffracting crystals of soluble proteins, I, understandably, had very limited access to the X-ray equipment at Martinsried. As a consequence, I spent four months at the MRC in Cambridge, England, together with Richard Henderson in 1980, in order to perform X-ray experiments. This period was essential for improving the crystallization method. After my return Dieter Oesterhelt decided to buy an X-ray generator for the ongoing work with bacteriorhodopsin. The generator was installed in Robert Huber's department and guaranteed us continued access to the equipment, and the know how, of the X-ray crystallographers. Later on, I used this generator for the work with the reaction centres.

Frustrated from the lack of the final success with bacteriorhodopsin, I tried to crystallize several other membrane proteins, mainly photosynthetic ones. After developing a new isolation procedure I obtained the first crystals of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis at the end of July 1981. One week later our daughter Andrea was born. During September 1981 the first reaction centre crystal was X-rayed by Wolfram Bode and myself, and turned out to be of excellent quality. Therefore 1981 was the happiest and most successful year of my life.

Dieter Oesterhelt immediately agreed that the reaction centre should be a project of the young people. In February 1982, I started the data collection for the X-ray structure analysis. In April or May I gave a seminar in Robert Huber's department and asked officially for collaboration. After some internal discussions Robert Huber agreed that Johann ("Hans") Deisenhofer, who was the partner of my choice, should take part in the reaction centre project. During the work Hans and I became the best friends. In August 1982, Hans and Kunio Miki, a Japanese post-doctoral research associate in Robert Huber's department, started to evaluate the pile of X-ray films. I continued with the experimental work, occasionally helped by Robert Huber, who showed me how the diffraction pattern of a promising derivative should look like. Not only the X-ray work, but also the entire biochemical characterization and sequence determination had to be done. After the preliminary tracing of the peptide chains by Johann Deisenhofer, the sequence determination, which was performed by Karl A. Weyer, Heidi Gruenberg and myself with Dieter Oesterhelt's support and help, turned out to be the bottle neck for our progress. During that period of heavy work our son Robert Joachim was born in 1984.

As one of the results of the success I received many offers. I accepted the one to become a department head and director at the Max-Planck-Institut für Biophysik in Frankfurt/Main, West Germany, where I am since October 1987.

For the success with the crystallization of membrane proteins and the elucidation of the three-dimensional structure of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis I received various prizes and awards. Among these are the Biophysics Prize of the American Physical Society (together with d. Deisenhofer), the "Chemiedozentenstipendium" of the "Fonds der Chemischen Industrie", the "Otto Klung-Preis" for chemistry, the Leibniz-Preis of the Deutsche Forschungsgemeinschaft, the "Otto-Bayer-Preis" (together with J. Deisenhofer) and now the Nobel Prize (together with J. Deisenhofer and R. Huber).

From Nobel Lectures, Chemistry 1981-1990, Editor-in-Charge Tore Frängsmyr, Editor Bo G. Malmström, World Scientific Publishing Co., Singapore, 1992

This autobiography/biography was written at the time of the award and first published in the book series Les Prix Nobel. It was later edited and republished in Nobel Lectures. To cite this document, always state the source as shown above.

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	Alan Fersht, FRS UK , Group Leader, MRC Laboratory of Molecular Biology, University of Cambridge Protein Folding Misfolding p53 and Cancer

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	Richard L. Atkinson, M.D. graduated from the Medical College of Virginia, Richmond, and trained in Endocrine-Metabolism at UCLA-Harbor General Hospital, Torrance, CA, and Walter Reed Army Hospital. He is Clinical Professor of Pathology, Virginia Commonwealth University; Editor of the International Journal of Obesity and of Nutrition and Diabetes; and a Member, Board of Directors, International Association for the Study of Obesity. He is the owner of Obetech, LLC, Richmond, VA. This company sells diagnostic tests for adenoviruses that produce obesity and other diseases. Obetech has multiple patents in the area of virus-induced obesity, diagnostic assays, antiviral agents, and vaccines.

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	Dr. Debomoy K. Lahiri in the Department of Psychiatry and of Medical & Molecular Genetics and full member of the Stark Neurosciences Research Institute at the Indiana University (IU) School of Medicine, Indianapolis, USA. Currently, he is Chief of the Laboratory of Molecular Neurogenetics at the Institute of Psychiatric Research of IU School of Medicine. Prior to joining Indiana University, Dr. Lahiri was a faculty member at Mount Sinai School of Medicine, New York, NY. His particular research interest is to understand the mechanism of aging; origin and biogenesis of the amyloid plaque and gene regulation of Alzheimer's disease (AD). Dr. Lahiri has been working in the neurobiology and genetics of AD and molecular biology of β-amyloid precursor protein (APP), synaptic proteins and other AD-related genes for over 20 years. He is also studying the novel role of microRNAs (miRNA) in brain disorders, such as AD. Further, Dr. Lahiri’s group has recently shown beneficial effects of dietary nutrients, such as aged garlic extract (AGE), S-Ally cysteine (SAC), and nanocurmin in neuropreservation and neuroprotec-tion, which have far reaching implications in man’s health and longevity. Dr. Lahiri has been awarded multiple research grants as a Principal Investigator from the National Institute on Aging, NIH, and Alzheimer's Association. Dr. Lahiri is a member of the NIH study section, of the Scientific Advisory Board for the Institute for the Study of Aging, New York, for QR Pharma, Philadelphia and for Yuma Therapeutics, Boston. He has published over 250 scientific papers in the field of neurobiology, genetics and AD (including high impact factor journals, such as JBC, PNAS, FASEB J, JPET, Neuron, and Nature Neurosci Rev and Science). Dr. Lahiri is the Editor-In-Chief of the international journal, ‘Current Alzheimer Research', which is listed in MEDLINE/PubMed (www.benthamscience.com/car). He has also coauthored books, such as ‘Protective Strategies for Neurodegenerative Diseases' published by the New York Academy of Sciences. Dr. Lahiri's honors include the listing in Marquis' ‘Who's Who in the World', and receiving the prestigious ‘Zenith Award' from Alzheimer's Association.

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	DQ. Ping Dou ,Ph.D Professor Barbara Ann Karmanos Cancer Institute Departments of Oncology, Pharmacology and Pathology School of Medicine Wayne State University 540.1 Hudson Webber Cancer Research Building Mail code HW05AO 4100 John R Road Detroit, MI 48201-2013 Tel: 313-576-8301 (Office); 313-576-8299 (Adm. Assistant); 313-576-8264, -8248, -8249 (Lab) Fax: 313-576-8307 (Office); 313-576-8928 (Adm. Assistant) E-mail: doup@karmanos.org

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	Dr. Taleb Al-Tel received his BS in Chemistry and Chemical Technology in 1987, MS in Natural Product Chemistry in 1990 from the faculty of Chemistry, Jordan University, and PhD in 1995 from The University of Tuebingen-Germany under Professor Wolfgang Voelter followed by an NIH Postdoctoral Fellowship at State University of New York, Stony Brook, NY. Dr. Al-Tel joined Transtech Pharma-USA Drug Discovery and Development in 2004 as principal scientist and advanced through roles of increasing responsibility to TeamLeader. In this position, he has built a strong multi-disciplinary Chemical & Screening Sciences (CSS) organization. During his tenure he has fostered a highly creative environment based on modern drug discovery technologies and enhanced chemistry skills and capabilities via the recruitment of high caliber scientists. In his current role at the college of Pharmacy-University of Sharjah as associate professor of organic and medicinal chemistry, he oversees Sharjah Chemistry and Discovery research efforts of many0 scientists at the Sharjah Institute for Biomedical Research.

Pharma R&D Achievements: Over the years his research efforts led to the discovery of many clinical drug candidates and many compounds currently under clinical evaluation including: BACE1-Inhibitor-Alzheimers; AGRP-Obesity, I7L-Anti-viral.

Scientific Contributions include over 150 invited lectures, presentations and publications; inventor on a one US-issued patent. Awards include: Abdel Hameed Shoman Prize for Young Arab Researchers (1999), Islamic Development Bank Award (2003), Fulbright Award (2003/2004), The Best Research Article Award-University of Sharjah-2010, University of Sharjah Incentive Award for Research Achievements-2009, University of Sharjah Best Research Project Award-2012, Suma Cum Laude Ph. D. Award-Tuebingen University-1995, Mango Award-University of Jordan-1987-1989, Jordanian Higher Education Council Award-1989, ISESCO Research Visit Award-1990, The Chemist of the Year Award-2005, TransTech Pharma-USA.

Scientific and Professional Activities include Mini Reviews on Medicinal Chemistry Advisory Board member, Open Journal of Natural Products Advisor Board member, Journal of Organic Chemistry Research Editorial Board member, World Journal of Translational Medicine Editorial Board Member, AAAS-member, ACS-member, The Royal Society of Chemistry (FRSC)-member, and frequent reviewers of many international journals including, JMC, JOC, BOC, Tetlett, EJMCHM…etc.

Academic Appointments: Professor of Organic Medicinal Chemistry, Chairman/Department of Medicinal Chemistry College of Pharmacy, University of Sharjah, Invited Visiting Professor at many Schools including, Tuebingen University-Germany, Molecular Pharmacology Research Institute-Berlin, Ecole-Normale Superior-Paris.

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	Harald zur Hausen MEAT AND MILK PRODUCTS OF DAIRY COWS AS RISK FACTORS FOR CANCERS AND NEUROLOGICAL DISEASES Deutsches Krebsforschungszentrum Im Neuenheimer Feld 280, 69120 Heidelberg, Germany

Slightly more than 20% of the global cancer incidence is linked to viral, bacterial, or parasitic infections. Their discovery permitted novel approaches to cancer prevention either by vaccination (Hepatitis B and human papillomaviruses) or by therapeutic interference with persistent infections (HIV, Hepatitis C, Helicobacter pylori, Schistosoma and liver flukes). These developments encourage further research on a potential involvement of other infections in cancers, not yet linked to exogenous agents. We presently study the putative role of novel viruses in cancers of the colon and the breast, but also in multiple sclerosis (MS). Epidemiological studies suggested a possible role of infectious events in these malignancies and MS, probably due to consumption of bovine infected meat and dairy products. A number of novel single-stranded DNAs have been isolated from bovine serum and milk, but also from individual multiple sclerosis lesions. They are presently being analysed for a possible role in these cancers and neurological diseases.