CHEMICAL SCIENCE AND ENGINEERING AT BERKELEY
Newsletter of the College of Chemistry, University of California, Berkeley
Volume 9, Number 3, August 2001
College Construction Update
Or "How much longer is this drilling going to last?"
Yes, the jack-hammering can seem interminable.
But Susan Slavick, the Building Manager for
the College of Chemistry, assures us that there
is an end in sight. And when it is all over, both
Hildebrand and Latimer will be upgraded for
seismic structure and life safety, with automatic
fire sprinklers installed in all the offices and
labs.
IN THIS ISSUE:
New faculty
profiles:
Jamie Cate..........2
Matt Francis........3
Jay Groves..........4
John Kuriyan.......5
Michael
Marletta.............6
Faculty Updates
& Noteworthy
News ..................7
“I think the progress made by Rudolph and
Sletten, the on-site contractor, is clear, with the
many concrete pours outside both buildings and rods
sticking out of Latimer. So far everything is pretty
much going according to schedule, and the projects
should be completed in the spring of 2002,” Slavick
said. The labs on the second and third floor of
Hildebrand will then provide surge space for the scientists who will be vacating Stanley as construction
for its replacement building begins.
In addition to the seismic upgrades and the renovation of several “surge” labs, other large construction
projects around the Chemistry Complex are also near-
Changing Faces at Latimer
Upcoming
Events..................8
In Memoriam:
Andrew Dorsey....8
Photos by Jane Scheiber
The College of Chemistry bade a fond farewell to
long-time staff members (above, left to right) Betty
Rancatore, who retired as Chemistry Management
Service Officer (MSO) after over 26 years at the university; Irene Katsumoto, who retired after 11 years
of service, most recently as Assistant to the Dean;
and Rebecca Pauling, who transferred to Integrative
Biology after 10 years with Chemistry. Betty was presented with the Berkeley Citation.
ing completion. “The Marletta labs in Lewis will be
ready at the end of August, and the second phase of
the Bertozzi labs on the eighth floor of Latimer will be
completed in October,” Slavick said.
“The faculty and staff members have dealt with all of
the noise and hubbub incredibly well,” Slavick added.
Dean Heathcock commended Slavick for “an outstanding job in keeping everyone informed so they
could plan their schedules to avoid the worst of the
noise and vibration.”
“The complaints have been minimal and the building
occupants have been fantastic—patient and understanding. This will greatly contribute to the final overall success of this very complex and difficult project,”
Slavick said.
The website http://www.cchem.berkeley.edu/
~physplnt/Seismic/retrofit.html offers photos and updates of the seismic project as well as a three-week
rolling schedule, so you can find out where the noise
and dust will be ahead of time.
Joel Nice (below left), formerly with the Electronic
Research Lab, is the new MSO for Chemistry. He
assures us that he is enjoying the many challenges
of his job. Rebecca Egger (below, center) is the new
senior analyst and Assistant to the Dean. She comes
to the College from the University of Michigan, where
she was a member of the English Department faculty.
This new position, in addition to academic personnel, will involve high-level analysis for the Dean on a
broad range of issues. Adam Lieb (below right) is the
new Assistant Building Manager.
www.cchem.berkeley.edu
New Faculty Members Bridge Chemistry and Biology
Jamie Cate: Protein Synthesis 101
Assistant Professor Jamie Cate could
be a poster boy for the benefits of undergraduate research. “I was interested in chemistry back in high
school and majored in it as an undergraduate. But I was
getting bored with the classes. The professors stressed
rote memorization, and while I was good at it, it wasn’t
much fun. Luckily, I started working in a lab with a good
professor who really communicated to me that science
was an ongoing process that was both exciting and unpredictable.”
Cate, who has a joint appointment with Molecular and
Cell Biology, still exudes enthusiasm talking about his
research. “I’m interested in ribosomes and protein synthesis, one of the most fundamental biological processes,”
he explained. “Protein synthesis is conserved in all organisms, from bacteria up through to humans.” Our genetic information is stored in DNA. However, in order for
that information to ultimately lead to cells, tissues and people, the
DNA is first transcribed into messenger RNA (mRNA), which travels out of the nucleus and is translated by the ribosome into proteins.
are not purified with the ribosomes, such as EF’s, elongation factors, and the associated mRNA and tRNA, are purified individually
and added back to the system later. “We add back only the pieces
of the puzzle that we want to study,” he said.
“Decoding is the next process to look at,” Cate said.
Decoding is the actual reading of the set of three
nucleotides, known as a codon, in the mRNA, that
codes for an amino acid. The ribosome protein factory moves along the mRNA three nucleotides at a
time, reads that codon, and using the correct tRNA,
attaches an amino acid at the right place in the growing protein chain. The ribosome then moves to the
next codon and begins again.
“It sounds like a simple process but there’s much
that we don’t even begin to understand. Like, how
does the tRNA get chosen, and how does the ribosome move from
one tRNA to the next? We know that the elongation factor EF-Tu
and the small molecule GTP are involved in choosing the tRNA.
We also know that EF-G and GTP are involved in the ratcheting of
tRNA through the ribosome.”
“For decades we have studied the ribosome using genetic and
“In order to crystallize these complex protein assemblies in very
biochemical means, but the structure was not known until recently.”
defined states, we use a number of little tricks,” Cate explained.
In a breakthrough Science paper last year in collaboration with
One is using antibiotics that muck up translation by locking the
Harry Noller at UC Santa Cruz, Cate and colribosome in a very specific conformation.
leagues described the crystal structure of the
“We can also use analogs of GTP that
Cate and colleagues described the crystal
complete Thermus thermophilus bacteria 70S
cannot be hydrolyzed, which trap the ristructure of the complete Thermus
ribosome containing bound messenger RNA
bosome in certain states.”
thermophilus bacteria 70S ribosome
and transfer RNAs (tRNAs) at an astonishcontaining bound messenger RNA and
ing 5.5 angstrom resolution. tRNA is a pro“There are dozens of accessory factors
transfer
RNAs (tRNAs) at an astonishtein that "reads" the mRNA in the ribosome
involved in ribosome function in humans.
ing 5.5 angstrom resolution
and attaches the correct amino acid to the
We want to first develop a comprehengrowing protein.
sive model using the bacteria E. coli and
The details seen in the 5.5 Å resolution pictures of the ribosome
included the major and minor grooves of RNA double helices. Cate
and his colleagues also identified the positions of tRNA in three of
its binding states and observed many of the ribosomal proteins.
Further, they could distinguish single strands of the RNA, even in
the double-helical regions.
“Getting that kind of resolution of such a complex protein factory
allows us to ask all sorts of interesting questions now,” Cate remarked. “Like how does the ribosome read the genetic code and
choose the correct tRNA? How do certain antibiotics cripple bacterial ribosomes and distinguish between mammalian ribosomes
and their bacterial targets?”
Bacterial ribosomes have 50–60 parts and can be purified gently so
that they emerge intact and functional. The accessory factors that
www.cchem.berkeley.edu
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are collaborating with groups such as Adam Arkin’s. Their computational expertise complements our molecular biology research in
understanding these complex systems,” Cate said.
A native of Colorado, Cate received his B.S. in chemistry from the
University of Denver in 1990. He earned his Ph.D. in 1997 from Yale
University, studying the structure of catalytic RNAs with Jennifer
Doudna, and was a postdoc with Harry Noller at UC Santa Cruz.
After two years as an Associate Member of the Whitehead Institute and Assistant Professor at MIT, Cate has now moved his lab
to UC Berkeley.
“I do a fair amount of structural studies and Berkeley has great
facilities for my experiments, including the ALS (Advanced Light
Source at LBNL), which is well suited for structural biology studies. Of course the great restaurants here and close proximity to
outdoorsy activities like hiking don’t hurt," Cate said.
New Faculty Members Bridge Chemistry and Biology
Matt Francis: Designer Proteins
Assistant Professor Matthew (Matt) Francis is a familiar face to the
chemistry department. Francis has spent the last two years as a
postdoctoral fellow with Professor Jean Fréchet, designing new
polymers to improve existing methods of drug delivery and developing methods to attach them to
strands of DNA.
“There are lots of variables to take into
account,” Francis explained. “But I
have always been interested in building and engineering, and I think doing
organic synthesis is like being an architect. You first learn the basic tools
and reactions that can be used to construct very complex structures.”
Growing up in rural Ohio, Francis received his B.S. in chemistry from Miami University in 1994. He obtained his Ph.D. in 1999 at Harvard
University, studying asymmetric catalysis under Prof. Eric Jacobsen,
before assuming his postdoctoral position here.
“I was delighted to have the opportunity to continue here as a
faculty member because of the diversity of the research that occurs
on campus and in the college. Berkeley offers a tremendous opportunity for collaborations,” Francis said. Chemistry is becoming
increasingly interdisciplinary and the more diversity in a department, the stronger
that department is,
Francis believes.
“I realized that organic chemists are in a
“My goal as a facunique position to combine the two fields of
ulty member is to
materials and biology.”
continue to branch
out as a chemist and
choose projects that
stretch the boundaries of chemistry
into other fields. After graduate school, I thought that as a synthetic chemist I had to choose whether to expand into materials
science or biology. But as I progressed in my studies and research,
I realized that organic chemists are in a unique position to combine
the two fields of materials and biology. So far it has been fun to
bridge these traditionally distinct disciplines,” Francis remarked.
According to Francis, finding new ways to construct a molecule is
quite a challenge. “In the Fréchet group, we did a lot of work constructing conjugates of DNA with polymers known as dendrimers,
which are well-defined branched polymers with many interesting
uses,” he said. “The DNA portion selfassembles, taking the shape of a doublehelix. And that got me thinking about where synthesis should go,
especially with nanoscale materials. Can self-assembly be harnessed
to synthesize molecules on a length scale compatible with nanoscale
science? Self-assembling proteins have well-defined side chains
that can be modified, allowing us to add new functions, with a
growth mechanism built right in. If we can harness that property
and control where the protein polymers begin and end, we can use
that knowledge to build useful things such as circuits.”
Another aspect of self-assembling proteins is that they assemble
in complex three-dimensional patterns that are incredibly difficult
to synthesize with standard technology. “I intend to use the selfassembling proteins of viruses and modify those proteins on both
their inner and outer surfaces,” Francis said. In nature these viral
proteins assemble into different geometries, one of the most familiar of which is the icosahedron, which has twenty sides. If we can
place short polymers on the outside of these structures without
affecting their ability to assemble, we could effectively discourage
an undesired immune response in drug delivery applications. We
could also modify these proteins to carry drug molecules inside the
protein shell, effectively making the virus a Trojan horse. The drugs
would be encapsulated and delivered using vectors already used
by nature.”
“I plan to isolate proteins from natural sources and then carry out
synthesis on the surface,” Francis stated. “This path could lead to
whole new types of devices and methodologies. There is a lot of
excitement in the scientific community about nanoscale science
because it is brand new, but where nanoscale science will go in the
future is impossible to say.”
Contemplating his future endeavors, Francis remarked, “In my research, I would like to look back someday and realize that I have
helped develop a toolkit that allows researchers to access selfassembling proteins and control them in useful ways. Materials
scientists are conventionally thought of as shrinking things down
to make such things as faster microprocessors, and this has proven
to be a very important challenge. But there are a lot of other interesting things that we could do by building from the ground up.”
“In my spare time (I have spare time?) my wife and I enjoy doing
outdoor things, such as camping, hiking and backpacking. I also
enjoy cooking. My best recipe is a dry gin martini, two olives,
straight up, though I suppose I shouldn’t tell incoming students
that!” Francis laughed.
www.cchem.berkeley.edu
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New Faculty Members Bridge Chemistry and Biology
Jay Groves: How Cells Recognize Each Other
Groves studies how cells recognize each
other. “Cell membrane recognition is involved in such phenomena as cell signaling, the immune system, and development,”
he explained. “As a faculty member, I will
develop new strategies to image and study
the dynamic spatial organization of molecular components in cell membranes. The membrane is an attractive object of study because it is a two-dimensional fluid embedded in a three-dimensional space. Also, membranes are the definitive organizational
motif for life. I think we can learn a lot about how a collection of
molecules comes to life by studying membranes. We are one of the
only groups approaching this topic from a physical chemistry point
of view. Until recently it has been the domain of cell biologists.”
and structure on lipid membranes,” he said. This is a fairly general
technique that yields lipid membranes with precisely defined patterns. “The aim of this research is to develop micropatterned membranes and other more general structures to help us study the role
of dynamic organization in cell membranes. This project involves a combination of several rather different
technologies. First, conventionally
microfabricated substrates are used
to guide the assembly of membranes
and proteins into desired geometries.
These hybrid bio-solid-state structures are then used to study proteins
and living cells.”
Peg Skorpinski
Though he has been on the faculty since
summer of 2000, Assistant Professor Jay
Groves is considered a recent addition to the chemistry department. He spent his first year as a professor on leave to complete a
fellowship at the Lawrence Berkeley National Labs. “I was halfway through my
appointment as a Division Director’s Fellow, which has a two-year appointment. It
is a recently created fellowship initiated by
Graham Fleming and proved to be a really
great experience for me,” Groves said.
“I find it fascinating that the cell can
take a few simple interactions and use
them to form complex behavior,”
Groves said. There are a relatively
small number of chemical interactions
that occur on the cell surface, and
cells use this limited repertoire to recognize and communicate with
each other extremely accurately. Scientists on the campus are investigating many of these interactions.
“I chose to come to Berkeley because it has the strongest chemistry department in the country and is very strong in physical chemistry,” he explained. “The department has the facilities and the
resources I need, and it is constantly attracting outstanding students and researchers.”
Working with collaborators, including Chemical Engineering Chair
Arup Chakraborty, Groves has uncovered a novel mechanism that
immune cells use to respond to specific arrangements of cell surWhen he is not doing science, and sometimes when he is, Groves
face proteins. “We discovered the interesting fact that immune
travels around the world. Afcells react to self-organizing patterns of cell surface
ter receiving his Ph.D. under
receptors, not the receptors themselves,” he said.
“The membrane is an attractive object of
Steven
Boxer from Stanford in
The receptors for the immune cells reorganize themstudy because it is a two-dimensional
1998,
Groves
spent a year in
selves in response to certain stimuli. The immune
fluid embedded in a
Taiwan
as
a
visiting
scholar.
cells then recognize the changing pattern of their
three-dimensional space.”
“I
love
to
travel.
I
spent
a lot
receptors and thus recognize the cell. It is analogous
of
time
wandering
throughout
to gaining information by reading a string of letters
China and India. I actually
from left to right to comprehend a sentence, rather
brought my laptop computer
than just counting the number of letters present.
with me to Beijing, China and
"This finding leads to some quite interesting results," Groves confinished writing my thesis there. In Taiwan, I was supported by a
tinued. "For example, if we examine observations made by cell biTaiwanese governmental fellowship, which allowed me to do some
ologists over the past decade and apply our models for self-orgatheoretical chemistry work and spend the rest of the time improvnizing patterns, we can begin to understand the molecular laning my Mandarin,” he said.
guage that cells use to communicate. And the experimental results
“I find that traveling stimulates my mind. Recently I went on a solo
support us. This approach represents a fundamental change in
trek through the Patagonian Andes of southern Chile," he said. "I
thinking about cell-cell recognition.”
also enjoy windsurfing. The Bay Area has some of the best
windsurfing available. I think my favorite place is underneath the
“My lab also uses microfabricated substrates to impose patterns
Golden Gate Bridge, where the views are just amazing.”
www.cchem.berkeley.edu
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New Faculty Members Bridge Chemistry and Biology
John Kuriyan: Signaling for a Change
After fourteen years at the
Rockefeller Institute in New
York, Professor John
Kuriyan is coming to Berkeley. “There are a lot of reasons I wanted to move out
west,” said Kuriyan, a
Howard Hughes Medical Investigator who was recently
elected to the National Academy of Sciences. “I wanted
to experience being at a large
American university. The Rockefeller Institute is a small community that trains only graduate students. I found that I wanted to
teach undergraduate courses, which I enjoyed doing when I was a
graduate student. Also, the research at the Rockefeller Institute is
focused primarily on biological issues, which suited me fine for
quite a while. But I am at a point in my career where I want to better
integrate chemistry and biology, and Berkeley is renowned for the
close interaction between the two disciplines,” he explained.
In the past ten years, laboratories around the world, including
Kuriyan’s, have made amazing progress using molecular and cell
biology and X-ray diffraction to determine the structures of complex protein assemblies at atomic resolutions not thought possible
by previous generations. “We can study signaling processes and
proteins involved in DNA replication, the copying of DNA by the
cell before it divides, at less than 3 Å,” he said. “We can gain a lot
of useful knowledge by knowing a protein’s structure. I am interested in complementing the structural data with more functional
analyses. I want to know how certain proteins known as motor
proteins use chemical energy to change the structure of other proteins and effect major changes.”
Kuriyan studies the molecular machines and switches that carry
out signaling and DNA replication in the cell. Molecular biologists
have determined many of the genes and proteins involved in cell
signaling, according to Kuriyan. The next step is to understand
what regulates the interaction between different molecules. “The
challenge of studying cell signaling is that we essentially do not
understand the grammar and spelling of cell communication, but
we know which letters they use,” he said, comparing cell signaling
to language.
“Our laboratory focuses on how phosphorylation influences the
properties of proteins,” he said. Phosphorylation is the process in
which a signaling protein known as a kinase adds a small chemical
group to its target protein, thus changing its shape and its ability
to function. “The signaling proteins we study include kinases such
as Abl and Src. Kinases are crucial in signal transduction path-
ways that control cell growth, cell death
and other processes,” Kuriyan noted.
“My lab, along with Stephen Harrison’s at Harvard, determined
the first three-dimensional structure of c-src, a kinase important in
the development of certain cancers such as breast and colon. We
plan to do computer modeling as well as mutagenesis studies to
better understand c-src and other kinases,” he said.
In one recent study, Kuriyan and colleagues used x-ray crystallography to discover how the anticancer drug STI-571 from Novartis
Pharmaceuticals Corporation inhibits the Abl kinase. In chronic
myelogenous leukemia (CML), the Abl kinase, which is normally a
well-behaved cellular switch, becomes over activated by a
rearrangement of chromosomes during blood cell development.
The genes Abl and Bcr are normally found on two different chromosomes. However, these
chromosomes can become
“The challenge of studying
linked together, resulting in a
cell signaling is that we
fusion Bcr-Abl enzyme that
essentially do not understand
stimulates white blood cells
the grammar and spelling of
to grow without any regulacell communication.”
tion and leads to leukemia.
“The regulation of the Abl
kinase has been a major
puzzle that we have worked on for many years,” Kuriyan said in a
press release by the Howard Hughes Medical Institute. “In particular, we were interested in the fact that although the Abl gene is
very similar to the well-known Src family of oncogenes that also
produce kinases, the drug STI-571 inhibits Abl but not the Src
kinases.”
Analysis of the combined structure of STI-571-Abl and the additional biochemical experiments produced some surprising results,
Kuriyan continued, because they revealed that STI-571 bound only
to inactivated Abl and did not recognize the activated form. The
studies showed that STI-571 targeted the Abl protein only when a
key Abl structure, called an activation loop, was shut down. “Basically, we demonstrated that STI-571 is binding to Abl in its off
position, but not when the activation loop is in its on position,”
said Kuriyan. Thus, he emphasized, the drug’s preference for Abl
over Src can be explained by the difference in the shapes of inactivated Abl and Src.
In his move out west, Kuriyan is actually uprooting sixteen people
from Rockefeller, as well as his family and his dogs. Currently shuttling back and forth between Berkeley and New York, Kuriyan will
settle here in October.
www.cchem.berkeley.edu
5
New Faculty Members Bridge Chemistry and Biology
Michael Marletta: NO toxicity? No problem
Professor Michael Marletta is in the process of moving his lab to Berkeley from
the University of Michigan. Marletta , recently elected a fellow of
the American Academy of Arts and Sciences, is eager to begin his
research here. “I am really excited to be back in the Bay Area. I
received my Ph.D. from UCSF and fell in love with this part of the
country years ago. It's hard not to love it here.”
“The main project in the lab is
the study of nitric oxide (NO)
as an intracellular signaling
agent,” Marletta said. NO
serves many functions in the
body, such as causing blood
vessels to dilate, and it is capable of killing bacteria, fungi,
and even tumor cells. However, it is also very dangerous
at high levels because it is a
toxic nitrogen free radical. NO
can actually kill neurons and
is thought to be responsible for much of the degeneration that
occurs after strokes and in some neurological diseases such as
Huntington’s and Alzheimer’s.
“The idea that nature would use a toxic agent such as NO as a
signaling agent was considered preposterous until the science
was worked out in the mid-to-late '80s,” he remarked. “However,
we now know that NO plays an extensive and important role in
mammalian biochemistry,” Marletta explained. “What I want to understand is how exactly NO works: how the enzyme nitric oxide
synthase forms NO, how NO finds its target, which happens to be
another enzyme, how the binding of NO occurs, and how the receptors in the cell bind and distinguish NO from other small compounds, such as O2. My lab is working out the many questions of
NO signaling at the molecular and atomic levels.”
“We are also studying how NO is used by humans as a protection
against invading bacteria. Say you cut yourself chopping onions:
bacteria enter the cut and start multiplying. But white blood cells in
your immune system bombard those bacteria with several noxious
chemical compounds including NO and kill the bacteria,” Marletta
continued. “However, many pathogens, such as Mycobacterium
tuberculosis, are resistant to NO. We are gathering evidence that
these pathogens contain enzymes that can degrade NO and
detoxify it. If we understand how these enzymes thwart NO toxic-
ity, we can work toward better treatments for diseases such as
tuberculosis,” he said.
Another project Marletta is pursuing involves the formation of
hemozoin by the malarial parasite. “The Plasmodium parasite that
causes malaria spends time in red blood cells, where it degrades
hemoglobin and uses the waste as a source of nutrition. The heme
molecule, which consists of a protoporphyrin ring and a central
iron (Fe) atom, is liberated from hemoglobin and would normally be
toxic to the parasite. But the malaria parasite contains an unusual
protein, the histidine-rich protein (HRP), which polymerizes the
heme to form hemozoin. And hemozoin is relatively harmless,” he
said. “I would like to understand what happens when this protein
binds to heme, how it polymerizes it to a nontoxic compound.”
According to Marletta, the HRP initially starts out in a random coil
configuration. However as it binds to heme, it slowly adopts an
unusual 3-10 helix conformation. “By modeling this binding, we
can determine which histidine residues are needed for the HRP to
bind the heme,” he continued. This line of questioning could lead
to better antimalarial drugs and help eradicate a disease responsible for more than two million deaths a year.
“My lab is working out
the many
questions of NO
signaling at the
molecular and atomic
levels.”
“I am looking forward to doing
science at Berkeley. The scientific environment here was a big
draw,” Marletta said. “And Berkeley has put into place several initiatives that indicate a
willingness to accommodate
faculty working at the interfaces of the traditional disciplines, such as chemistry and
biology.”
“My lab asks chemical questions about biological problems. I think
this is exactly the right time when the interface between chemistry
and biology will really blossom and come into its own,” he said.
“Many scientists might think I have a screw loose,” laughed
Marletta. “After all, I gave up a Howard Hughes Investigator position to come here. But I was really attracted to this position because of the tremendous strength of the chemistry department and
because I am a firm believer that the real excitement in research is at
the interface of the traditional disciplines.” Marletta also has appointments in Molecular and Cell Biology and at UCSF.
The NEWSLETTER OF THE COLLEGE OF CHEMISTRY at Berkeley is published several times each year to support the College’s
mission of providing excellent teaching, research and public service in the fields of Chemistry and Chemical Engineering.
Editor: Yvette Delahoussaye, (510) 642-6867
[email protected] 420 Latimer Hall, Berkeley, CA 94720-1460
printed on recycled paper 2001 College of Chemistry
6
Faculty Updates and Noteworthy News
Neil Bartlett, Professor Emeritus of Chemistry, has been
elected a Foreign Fellow of the Royal Society of Canada by
members of the Academy of Science. This year, only three
Foreign Fellows were elected on the basis of distinguished
accomplishments in their fields.
Alex Bell, Professor of Chemical Engineering, received the Award for Excellence in Academic Research from the
Northern California Section of the AIChE
in May. He is also current Chair of the
Council for Chemical Research.
Jay Keasling and Doug Clark, Professors of Chemical Engineering, organized the Engineering
Foundation Conference “Biochemical Engineering” held in July
2001 at Sonoma.
Carlos Bustamante was
recently named as the best
molecular mechanic in the
U.S. by Time magazine
Robert Bergman, Professor of Chemistry, has been selected to receive the
2001 Leete Award, sponsored by the
ACS Division of Organic Chemistry. The
award is given biannually and recognizes superior teaching
and research.
Carolyn Bertozzi has received the Donald Sterling Noyce
Prize for Excellence in Undergraduate Teaching, which was
awarded at this year's commencement ceremony.
Harvey Blanch, professor of Chemical Engineering, received
the Amgen Award in Biochemical Engineering in June.
Chris Cappa, a graduate student with Ron Cohen, received
a National Defense Science and Engineering Fellowship.
Howard Han, a student with Carolyn Bertozzi in the Chemistry Department, has received an ACS Organic Division Graduate Fellowship.
Jeff Long, Assistant Professor of Chemistry, has won the
2002 Wilson prize, which is given annually by Harvard University to a young chemist of outstanding promise. Long follows
in the footsteps of Professor Paul Alivisatos, who won the
award in 1994.
Kevan Shokat, Professor of Chemistry and a joint appointment with UCSF, received the Eli Lilly Award in Biological
Chemistry from the American Chemical Society.
Kian Tan, a member of the Ellman/Bergman group, has
been awarded the Bristol-Myers Squibb fellowship. Tan will
receive $30,000 for the academic year.
Professors Ignacio Tinoco and Carlos Bustamante published a Science paper on single-molecule experiments on
unfolding RNA. Bustamante, who also has an appointment in
MCB, was recently named by Time magazine as the best
scientist working in molecular mechanics today.
Stacy Named Associate Vice
Provost
Professor Angelica Stacy has accepted a
three-year appointment as Associate Vice
Provost for Faculty Equity and will help
implement the campus's Academic Affirmative Action Plan. Dr. Stacy has long
been concerned with issues concerning
the status of women faculty.
Dan Krauss
This year's departmental teaching awards, also conferred at
commencement, went to Professor Martin Head-Gordon in
chemistry and Dr. P. Henrik Wallman in chemical engineering.
Judith Klinman, Professor and Chair
of the Chemistry Department, was
elected to the American Philosophical
Society. Founded in 1743 by Benjamin
Franklin, the society is the oldest of its
kind in the country and is devoted to
the advancement of scientific and scholarly inquiry. She was also honored on
her 60th birthday by 40 of her former and
present graduate students and postdocs, who held a symposium in her
honor.
Balsara Seeking Chemistry Students
Chemical Engineering Professor Nitash Balsara is looking for a few
good chemistry students to join his research program and study
soft nanostructures that spontaneously self-assemble from the
liquid state. Balsara and his colleagues also develop the tools necessary to characterize these materials. The applications of his
research range from the development of new strategies for recycling polymer mixtures to enabling the use of soft polymers in
electronic and photonic devices. For more information, check his
research page: http://www.cchem.berkeley.edu/~npbgrp/
research_main.htm.
www.cchem.berkeley.edu
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In Memoriam: Andrew Dorsey
Our student Andy Dorsey unexpectedly died on Sunday, August
12, 2001 from the consequences of a brain hemorrhage. Andy was
jogging on Bancroft Avenue when he suddenly collapsed. He
was brought to Alta Bates Hospital where he underwent surgery
immediately. Despite the best efforts of his doctors, he passed
away five days later. His family was with him throughout his
valiant fight. Andy was 23 years old.
Our condolences go out to his family, friends and colleagues. A
memorial service will be held later this year. In addition to
chemistry and science, Andy had a wide range of outside
interests. He loved nature and went out to the mountains as
often as possible. He had a talent for languages and was always
called into action when style questions were raised. Andy will be
greatly missed by our group.
-Dirk Trauner
Assistant Professor of Chemistry
MARK YOUR CALENDAR
Kenneth S. Pitzer Memorial Lecture, Tuesday, September 4,
4:00 p.m., Pitzer Aud., Latimer Hall. Professor Gerhard Ertl, FritzHaber-Institut der Max-Planck-Gesellschaft. "Dynamics of
Reactions at Solid Surfaces." Sponsored by ICI.
Bayer Lecture, Wednesday, September 26, 4:10 p.m., Pitzer Aud.,
Latimer Hall. Professor Bernhard Palsson, University of California, San Diego. "The Phase Transition from In Vivo to In Silico
Biology."
Bristol-Myers-Squibb Symposium, Thursday, September 27,
11:00 a.m., Pitzer Aud., Latimer Hall. Professor Jon C. Clardy,
Cornell University. "Natural Products and Natural Product
Libraries."
Homecoming & Parents’ Weekend, September 28–30. Enjoy a
complimentary continental breakfast on September 29, hosted by
Associate Dean Herb Strauss, from 8:00 - 9:00 a.m. in 775 Tan Hall
followed by a lecture from Adam Arkin “Cellular Engineering:
Control of the Single Cell” from 9:00–10:00 a.m. in 180 Tan Hall.
Special Seminar, October 4, 3:00 p.m., O'Neill Room of The
Faculty Club. Eric Seaborg, science writer and editor. “Glenn
Seaborg: Perspectives from a Son Turned Colleague.”
www.cchem.berkeley.edu
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