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The
University Lecturer in Chemistry 2001-2002
Robert
R. Birge
Harold
S. Schwenk Sr. Distinguished
Professor of Biological Chemistry
University of Connecticut,
University Professor and Director, W.M. Keck Center for Molecular Electronics,
Syracuse University
Bob Birge
received his B.S. degree in chemistry from Yale University in 1968, his
Ph.D. in chemical physics from Wesleyan University in 1972, and was a
National Institutes of Health postdoctoral fellow at Harvard University
from 1973-1975. He was an Assistant and subsequently a tenured Associate
Professor of Chemistry at the University of California, Riverside (1975-1984),
and then served as Professor and Head of the Chemistry Department at Carnegie
Mellon University (1984 - 1987). He joined the faculty at Syracuse University
in 1988 where he was Distinguished Professor of Chemistry and Physics,
Director of the W. M. Keck Center for Molecular Electronics, and Research
Director of the New York State Center for Advanced Technology in Computer
Applications and Software Engineering. In January 2000, he joined the
faculty at UConn where he holds the Harold S. Schwenk Distinguished Chair
in Biological Chemistry. He continues as a University Professor and Director
of the W. M. Keck Center at Syracuse, and maintains research groups at
both UConn (molecular biology and spectroscopy) and Syracuse (Protein
Devices). He has served on the editorial advisory boards of four journals
and has co-chaired advisory panels for the NIH and the National Academy
of Sciences. His research is supported by the NIH, NSF, AFOSR, ARO, the
W. M. Keck Foundation and four US companies. In 1997, he was listed among
the fifty "Cyber Elite" by Time Digital for his work on protein-based
devices, and the use of these devices for computer memories and processors.
[He was ranked 26th, behind Bill Gates (#1) and Steve Jobs (#24), but
ahead of Steven Spielberg (#28) and George Lucas (#33).]
Professor
Birge will present three lectures during his visit to UWO.
**All
lectures will be in Room 193 Medical Sciences Building**
Monday,
March 11, 2002 3:00 p.m.
1. Protein-Based
Three-Dimensional Memories
Molecular
electronics offers a powerful and cost-effective path towards computer
miniaturization and the generation of neural and three-dimensional architectures.
Bioelectronics investigates the use of native and genetically modified
biomolecules and offers advantages because nature has often solved many
of the key problems through evolution and natural selection. This presentation
will explore the use of the protein, bacteriorhodopsin, in optical three-dimensional
memories. These memories store information using volume elements (voxels),
and provide as much as a thousand-fold improvement in effective capacity
over current technology. A unique branching reaction of a genetically
engineered protein is used to turn each protein into an optically addressed
latched AND gate. The use of site directed mutagenesis and directed evolution
to optimize the protein for data storage will also be discussed. Although
three working prototypes have been developed, a number of cost/performance
and architectural issues must be resolved prior to commercialization.
Tuesday,
March 12, 2002 3:00 p.m.
2.
Large-scale Associative Memories and Artificial Intelligence
The
human brain stores and retrieves information via association. Human intelligence
is intimately connected to the nature and enormous capacity of this associative
search and retrieval process. Creativity can be viewed as the association
of two seemingly disparate concepts to form a totally new construct. Humor
can be traced to resonant association across experiential boundaries,
and can be appreciated by examining why some bumper stickers are funny
while others are not. But computer programs have trouble deciphering bumper
stickers and remain incapable of true artificial intelligence. One problem
is that current computer hardware does not provide an optimal environment
for creating artificial intelligence. The source of the problem is the
serial nature of random access memories, and software cannot provide a
satisfactory work-around that does not introduce unacceptable latency.
This talk will focus on the design and construction of large-scale, protein-based
associative memories and the potential use of these memories to create
artificial intelligence.
Wednesday,
March 13, 2002 3:00 p.m.
3. The Nature
of the Chromophore Binding Sites of Cone Pigments
It
is generally believed that the photoreceptor systems of the three phyla
with image resolving eyes, mollusks, arthropods and vertebrates, evolved
independently. And yet all three have selected the identical chromophore,
11-cis retinal, as the photoactive component for both scotopic (dim light)
and photopic (color) vision. This observation is all the more surprising
because the absorption spectra of the cone pigments extend from the ultraviolet
to the far red of the visible spectrum. Apparently, nature has converged
on both an optimal chromophore but also the means to tune this chromophore
so that it absorbs light across a large energy band. Of particular interest
are the blue and violet cone pigments, because their wavelength selection
mechanism is the most difficult to understand. In this talk we will examine
how the protein tunes the bound chromophore to achieve absorption in the
uv and blues while simultaneously maintaining a high photochemical quantum
yield. Our studies have focused on two short wavelength cone opsins, frog
(Xenopus laevis) violet and mouse UV. The Xenopus violet cone (VCOP)
is a close evolutionary cousin of the human blue cone, and has a nearly
identical absorption maximum at 425 nm. By studying over forty site directed
mutants and chimera, we have mapped the primary mechanisms of wavelength
regulation in both pigments. Our results provide an interesting window
into how nature can simultaneously optimize both wavelength and photochemical
behavior.
Refreshments
served before talks
For more information
contact: Lars Konermann (519-661-2111
ext. 86313)
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