Professor Ronald M. Evans, The Salk Institute for Biological Studies received the Glenn T. Seaborg Medal on Saturday, November 5, 2005 on the UCLA Campus, following the Symposium “Nuclear Receptors and the Complex Journey to Obesity”
Michael Strong, who did not get his picture taken, was the winner of this year’s Poster Session
At the Symposium, Before Lunch
“Thirty Years of Ups and Downs”
as narrated by Alex Pines of U.C. Berkeley
After the Break, Frank Anet Introduced
Peter van Zijl
Peter discusses “Exploiting the NMR Signals of Mobile Proteins & Peptides for MRI”
11:30 a.m.
Ann McDermott
gave the last talk before lunch. Her topic:
“NMR Studies of Intrinsic Membrane Proteins”
Lewis Kay, University of Toronto, discusses
“NMR Approaches for the Study of Protein Structure & Dynamics”
After Lewis’ talk: Lewis Kay, Alex Pines, Peter van Zijl and Wayne Hubbell
After Robert Clubb introduced her, Dorothee Kern from Brandeis, gives the 4:00 p.m. talk “Enzymes in Action in the NMR Tube: Protein Dynamics during Catalysis”
Gerhard Wagner describes “NMR Approaches for Studying Proteins Involved in Gene Expression”
1:00 pm
Opening Remarks
Roberto D. Peccei,
Dean, Physical Sciences, UCLA
1:10 pm
Jesse H. Ausubel
Director, Program for the Human Environment
Rockefeller University
“Transport: The Past 2000 Years, the Next 100”
1:50 pm
John H. Seinfeld
Chair, Division of Engineering and Applied Science,
Caltech
“Mathematical Modeling of the Atmosphere: State-of-the Science”
2:30 pm
James M. Lents
Director, Environmental Policy and Corporate Affiliates Program
U.C. Riverside
“Growing Vehicle Population and its Impact on Urban and Global Environments”
3:40 pm
Mary D. Nichols
Secretary for Resources, State of California
“Transportation and Environment: Successes and Challenges for California”
4:20 pm
John H. Gibbons
Former Director, White House Office of Science and Technology Policy
“Environment and Transportation: Can We Weave the Threads into Tapestry?
Welcome and Acknowledgements
Chairman Emil Reisler
Introductions
Professor Christopher S. Foote
Reflections
Professor Daniel Kivelson
Remarks
Mrs. Helen Petrauskas
Vice President,
Environmental and Safety Engineering
Ford Motor Company
Presentation
Executive Vice Chancellor, Wyatt R. Hume
Acceptance Remarks
Dr. John P. McTague
Dr. John P. McTague has had notable careers in academia, government, and industry. He earned an undergraduate degree with honors in Chemistry from Georgetown University in 1960 and a Ph.D. from Brown University in 1965.
Dr. McTague began his professional career at the North American Rockwell Science Center and then joined the UCLA Department of Chemistry as an Assistant Professor in 1970. He soon rose to the rank of professor and became a member of the Institute of Geophysics and and Planetary Physics. Dr. McTague’s seminal research on the dynamics and interactions of condensed matter included the first observations of collision-induced light scattering, magnetoviscosity in magnetic colloids, and the collective dynamics of monolayer films. His theoretical and computational work highlighted the unique role of the body-centered cubic phase in crystallization and of the existence of orientational epitaxy in incommensurate films.
In 1982, Dr. McTague became the first cdhair of the National Synchrotron Light Source at Brookhaven National Laboratory. He then served at the White House as Deputy Director and then Acting Director of the Office of Science and Technology policy. In 1986, Dr. McTague joined the Ford Motor Company where he spent more than 12 years, first as Vice President, Research and then Vice President, Technical Affairs. At Ford, he established USCAR, a unique research collaboration involving Ford, Chrysler, and General Motors.
Dr. McTague is Chairman of the Board of Overseers of Fermi National Laboratory, serves as Co-Chair of the Department of Energy’s Advisory Board. He is a member of the National Academy of Enngineering and a Fellow of the American Physical Society and the American Association for the Advancement of Science. He was awarded an honorary doctorate from Brown University in 1997, and, in 1998, he was the recipient of the Pake Prize of the American Physical Society.
Paul Delos Boyer was born July 31, 1918, in Provo, Utah. He received a B.S. degree in chemistry from Brigham Young University in 1939 and obtained a Wisconsin Alumni Research Foundation Scholarship for graduate studies. Five days before leaving for Wisconsin, Paul married a beautiful and talented coed, Lyda Whicker. Together they have three children, Gail, Hali, and Douglas, and eight grandchildren.
After he received his Ph.D. degree in Biochemistry from the University of Wisconsin in 1943, he spent years at Stanford University on a war-related research project dedicated to the stabilization of serum alubumin for transfusions. He began his independent research career at the University of Minnesota and introduced kinetic, isotopic, and chemical methods for investigating enzyme mechanisms. In 1955, he received a Guggenheim Fellowship and worked with Professor Hugo Theorell on the mechanism of alcohol dehydrogenase. In 1956, he accepted a Hill Foundation Professorship and moved to the medical campus of the Universithy of Minnesota. In 1959-60, he served as Chairman of the Biochemistry Section of the American Chemical Society and in 1969-70 as President of the American Society of Biological Chemists.
Since 1963, he has been a Professor in the Department of Chemistry and Biochemistry at UCLA. in 1965, he became the Founding Director of the Molecular Biology Institute and spearheaded the construction of the building and the organization of an interdepartmental Ph.D. program. This institutional service did not diminish the creativity and originality of his research program, which led to three postulates for the binding mechanism for ATP synthesis: i.e. that energy input was not used primarily to form ATP but to promote the binding of phosphate and mostly the release of tightly bound ATP; that three identical catalytic sites went through compulsory, sequential binding changes; and that the binding changes of the catalytic subunits, circularly arranged on the periphery of the enzyme, were driven by the rotation of a smaller internal subunit.
