Caltech Students Named Goldwater Scholars

Two Caltech students, Saaket Agrawal and Paul Dieterle, have been awarded Barry M. Goldwater scholarships for the 2015–16 academic year.

The Barry Goldwater Scholarship and Excellence in Education Program was established by Congress in 1986 to award scholarships to college students who intend to pursue research careers in science, mathematics, and engineering.

Saaket Agrawal is a sophomore from El Dorado Hills, California, majoring in chemistry. Under Greg Fu, the Altair Professor of Chemistry, Agrawal works on nickel-catalyzed cross coupling, a powerful method for making carbon-carbon bonds. Specifically, Agrawal conducts mechanistic studies on these reactions, which involves elucidating the pathway through which they occur. After Caltech, he plans to pursue a PhD research program in organometallic chemistry—the combination of organic (carbon-based) and inorganic chemistry—and ultimately hopes teach at the university level.

"Caltech is one of the best places in the world to study chemistry. The faculty were so willing to take me on, even as an undergrad, and treat me like a capable scientist," Agrawal says. "That respect, and the ability to do meaningful work, has motivated me."

Paul Dieterle is a junior from Madison, Wisconsin, majoring in applied physics. He works with Oskar Painter, the John G. Braun Professor of Applied Physics, studying quantum information science.

"The quantum behavior of atoms has been studied for decades. We are researching the way macroscopic objects behave in a quantum mechanical way in order to manipulate them into specific quantum states," Dieterle says. Painter's group is studying how to use macroscopic mechanical objects to transform quantized electrical signals into quantized optical signals as part of the larger field of quantum computing, a potential next generation development in the field.

"The power of quantum computing would be immense," says Dieterle, who would like to attend graduate school to study quantum information science. "We could simulate incredibly complex things, like particles at the edge of a black hole. Participating in this physics revolution is so exciting."

Agrawal and Dieterle bring the number of Caltech Goldwater Scholars to 22 in the last decade.

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Barton Receives Highest Honor from American Institute of Chemists

The Gold Medal of the American Institute of Chemists (AIC) has been awarded to Jacqueline Barton, the Arthur and Marian Hanisch Memorial Professor of Chemistry and chair of the Division of Chemistry and Chemical Engineering. The award is the AIC's highest honor and recognizes "service to the science of chemistry and to the profession of chemist or chemical engineer in the United States."

Barton's research centers on the chemical and physical properties of DNA and their biological implications. Her group examines the chemistry of how electrons are conducted throughout a DNA molecule and how DNA-repairing enzymes can use this electron flow to locate mutations and mistakes in the DNA that could potentially cause cancers and diseases.

Barton received her PhD from Columbia University in 1978. She has been at Caltech as a professor since 1989. The recipient of numerous honors—including the 2010 National Medal of Science, a MacArthur Fellowship, and the National Science Foundation's Waterman Award—Barton also was awarded the 2015 Priestley Medal, the highest honor of the American Chemical Society, for her work on the chemistry of DNA.

 

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Monday, May 18, 2015
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Jupiter’s Grand Attack

John H. Richards, 1930–2015

John H. ("Jack") Richards, a professor of organic chemistry and biochemistry at Caltech whose research was focused on gaining a molecular understanding of the mechanisms of protein function, passed away on Thursday, April 23, 2015. He was 85 years old.

Richards used altered proteins obtained from the deliberate mutation of DNA—a process called site-directed mutagenesis—in combination with recombinant and cloning techniques, as well as chemically synthesized polypeptides (chains of amino acids) and their derivatives, to study the mechanisms by which proteins act as catalysts to perform the chemical reactions necessary to life. Among the proteins of particular interest to Richards were proteolytic enzymes that break apart other proteins; enzymes called lactamases that endow some microorganisms with antibiotic resistance; and DNA polymerases, the enzymes that build DNA molecules by assembling nucleotides.

Richards also worked in collaboration with Harry Gray, the Arnold O. Beckman Professor of Chemistry, and Jay Winkler, member of the Beckman Institute and faculty associate in chemistry, examining how proteins transport the electrons that are the cell's energy currency, including a class of copper-containing proteins called azurins that power certain types of bacteria. As Gray recalls, "Jack, Jay Winkler, and I worked closely together for over 25 years. He was the perfect collaborator, generous with his time. He taught Jay and me and our students the biology we needed to attack problems in biological inorganic chemistry. His work on engineering blue copper proteins opened the way for experiments in the Beckman Institute Laser Resource Center that shed light on the factors that control electron flow in respiration and photosynthesis."

According to colleague Douglas Rees, the Roscoe Gilkey Dickinson Professor of Chemistry at Caltech and an investigator with Howard Hughes Medical Institute, Richards was a "visionary" who helped drive the integration of chemistry and biology at the heart of contemporary biochemistry.

"What most struck me about Jack is he had this real style," Rees recalls. "He wasn't the sort of guy who was just going to crank through and try to wear some problem down. He liked coming up with a really clever, elegant solution to a problem. And early on, at a time when I think a lot of chemists were typically not very interested in biological problems, Jack had this fascination with biology and chemical mechanisms. He appreciated how the future of biology was rooted in chemistry, and he was the leader of the modern era of biochemistry in the chemistry division here."

Richards was born on March 13, 1930, in Berkeley, California, and earned a BA from UC Berkeley in 1951. As a Rhodes Scholar, he traveled to England to attend the University of Oxford, from which he obtained a BSc in 1953. He then returned to UC Berkeley for his graduate studies, earning a PhD in 1955.

After two years as an instructor at Harvard University, Richards came to Caltech in 1957 as an assistant professor. He spent the rest of his career at the Institute, with promotions to associate professor in 1961 and to professor in 1970. He was named a professor of organic chemistry and biochemistry in 1999. Richards was the chair of the faculty from 1991 to 1993. 

"Jack Richards was part of the fabric of Caltech and interdisciplinary science for more than 50 years," says Jacqueline K. Barton, the Arthur and Marian Hanisch Memorial Professor and chair of the Division of Chemistry and Chemical Engineering.

Over his career, Richards also served in a number of corporate and governmental advisory roles, including as a member of the board of the Huntington Medical Research Institute since 1999 and as a member of the Department of Energy's Basic Energy Science Advisory Committee (2001–13).

From 1985 to 2007, Richards was a corporate scientific adviser to the biotechnology company Applied Biosystems, now a part of Life Technologies. Applied Biosystems was the first company to commercially produce an automated DNA sequencing instrument—technology that was pioneered at Caltech by Leroy Hood (BS '60, PhD '68).

Richards also embraced his role as an educator and acted as a mentor to generations of undergraduate and graduate students, as well as to faculty, during his nearly six decades at Caltech. "He really liked being with students and was stimulated by that interaction," Rees recalls. "He was able to teach up to the very end. I think that meant a lot to him."

"Jack was a co-advisor for my thesis work and an incredible mentor. He joyously encouraged and supported risk taking and strongly influenced my entry into the protein engineering field," says Stephen Mayo (PhD '88), Caltech's William K. Bowes Jr. Leadership Chair of the Division of Biology and Biological Engineering and Bren Professor of Biology and Chemistry. "Jack's advice and mentorship didn't stop after I completed my degree. He was a great sounding board for discussing research directions, and he provided incredibly clear career advice that was often delivered with humorous anecdotes that made our sometimes intense discussions easier. I owe Jack a great deal and will miss him as a mentor and colleague but, most importantly, as a friend."

"It's hard to imagine the sort of changes that you would see in this, in any place, over 58 years," Rees adds. "It's a long baseline. But he liked brainstorming about new ideas and technologies. He was a key part of the biochemistry subgroup. If we were grappling with some issue and trying to figure out what the most prudent course of action was, he would often look at it from his unique perspective, and we would say, you know, that's right. He could really unite us. He leaves a hole."

Richards is survived by his second wife, Minnie McMillan, professor of molecular microbiology and immunology and professor of neurology at the University of Southern California's Keck School of Medicine. Richards also leaves behind four daughters from his first marriage (to Marian King), Kathleen Fraga of Grass Valley, California; Jennifer Welton of Belgrade, Montana; Julia Hart of Clayton, California; and Cynthia Clapp of Corvallis, Oregon; and four grandchildren.

He will be buried in Nevada City, California, where his grandfather and favorite uncle lived.

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Kathy Svitil
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“Freezing a Bullet” to Find Clues to Ribosome Assembly Process

Researchers Figure Out How Protein-Synthesizing Cellular Machines Are Built in Stepwise Fashion

Ribosomes are vital to the function of all living cells. Using the genetic information from RNA, these large molecular complexes build proteins by linking amino acids together in a specific order. Scientists have known for more than half a century that these cellular machines are themselves made up of about 80 different proteins, called ribosomal proteins, along with several RNA molecules and that these components are added in a particular sequence to construct new ribosomes, but no one has known the mechanism that controls that process.

Now researchers from Caltech and Heidelberg University have combined their expertise to track a ribosomal protein in yeast all the way from its synthesis in the cytoplasm, the cellular compartment surrounding the nucleus of a cell, to its incorporation into a developing ribosome within the nucleus. In so doing, they have identified a new chaperone protein, known as Acl4, that ushers a specific ribosomal protein through the construction process and a new regulatory mechanism that likely occurs in all eukaryotic cells.

The results, described in a paper that appears online in the journal Molecular Cell, also suggest an approach for making new antifungal agents.

The work was completed in the labs of André Hoelz, assistant professor of chemistry at Caltech, and Ed Hurt, director of the Heidelberg University Biochemistry Center (BZH).

 

 

"We now understand how this chaperone, Acl4, works with its ribosomal protein with great precision," says Hoelz. "Seeing that is kind of like being able to freeze a bullet whizzing through the air and turn it around and analyze it in all dimensions to see exactly what it looks like."

That is because the entire ribosome assembly process—including the synthesis of new ribosomal proteins by ribosomes in the cytoplasm, the transfer of those proteins into the nucleus, their incorporation into a developing ribosome, and the completed ribosome's export back out of the nucleus into the cytoplasm—happens in the tens of minutes timescale. So quickly that more than a million ribosomes are produced per day in mammalian cells to allow for turnover and cell division. Therefore, being able to follow a ribosomal protein through that process is not a simple task.

Hurt and his team in Germany have developed a new technique to capture the state of a ribosomal protein shortly after it is synthesized. When they "stopped" this particular flying bullet, an important ribosomal protein known as L4, they found that its was bound to Acl4.

Hoelz's group at Caltech then used X-ray crystallography to obtain an atomic snapshot of Acl4 and further biochemical interaction studies to establish how Acl4 recognizes and protects L4. They found that Acl4 attaches to L4 (having a high affinity for only that ribosomal protein) as it emerges from the ribosome that produced it, akin to a hand gripping a baseball. Thereby the chaperone ensures that the ribosomal protein is protected from machinery in the cell that would otherwise destroy it and ushers the L4 molecule through the sole gateway between the nucleus and cytoplasm, called the nuclear pore complex, to the site in the nucleus where new ribosomes are constructed.

"The ribosomal protein together with its chaperone basically travel through the nucleus and screen their surroundings until they find an assembling ribosome that is at exactly the right stage for the ribosomal protein to be incorporated," explains Ferdinand Huber, a graduate student in Hoelz's group and one of the first authors on the paper. "Once found, the chaperone lets the ribosomal protein go and gets recycled to go pick up another protein."

The researchers say that Acl4 is just one example from a whole family of chaperone proteins that likely work in this same fashion.

Hoelz adds that if this process does not work properly, ribosomes and proteins cannot be made. Some diseases (including aggressive leukemia subtypes) are associated with malfunctions in this process.

"It is likely that human cells also contain a dedicated assembly chaperone for L4. However, we are certain that it has a distinct atomic structure, which might allow us to develop new antifungal agents," Hoelz says. "By preventing the chaperone from interacting with its partner, you could keep the cell from making new ribosomes. You could potentially weaken the organism to the point where the immune system could then clear the infection. This is a completely new approach."

Co-first authors on the paper, "Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension," are Huber and Philipp Stelter of Heidelberg University. Additional authors include Ruth Kunze and Dirk Flemming also from Heidelberg University. The work was supported by the Boehringer Ingelheim Fonds, the V Foundation for Cancer Research, the Edward Mallinckrodt, Jr. Foundation, the Sidney Kimmel Foundation for Cancer Research, and the German Research Foundation (DFG).

 

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JCAP Receives a 5-Year, $75M Funding Renewal

On Monday, April 27, the Department of Energy (DOE) announced a five-year, $75 million renewal of the Joint Center for Artificial Photosynthesis (JCAP). JCAP's mission is to explore the science and technology of artificial photosynthesis to harness solar energy for the production of fuel.

JCAP is the nation's largest research program dedicated to the development of an artificial solar-fuel generation technology. Established in 2010 as a DOE Energy Innovation Hub, JCAP aims to create a low-cost generator to make fuel from sunlight 10 times more efficiently than plants. Such a breakthrough would have the potential to reduce our country's dependence on oil and enhance energy security.

The Hub is directed by Caltech, but it has its primary sites both at Lawrence Berkeley National Laboratory (LBNL) and at Caltech. JCAP brings together more than 150 scientists and engineers from Caltech and LBNL, and also draws on the expertise and capabilities of key partners at UC Irvine, UC San Diego, and the SLAC National Accelerator Laboratory at Stanford.

The funding renewal announcement was made at LBNL by Franklin Orr, under secretary for science and energy at DOE.

"JCAP's work to produce fuels from sunlight and carbon dioxide holds the promise of a potentially revolutionary technology that would put America on the path to a low-carbon economy," said Orr in a DOE press release. "While the scientific challenges of producing such fuels are considerable," the released noted, "JCAP will capitalize on state-of-the-art capabilities developed during its initial five years of research, including sophisticated characterization tools and unique automated high-throughput experimentation that can quickly make and screen large libraries of materials to identify components for artificial photosynthesis systems."   

"We are honored and delighted to receive renewed support from the Department of Energy for JCAP," says JCAP director Harry A. Atwater, Howard Hughes Professor of Applied Physics and Materials Science at Caltech. "Thanks to this renewal, JCAP will continue to push the scientific frontiers of artificial photosynthesis, with an emphasis on selective carbon dioxide reduction under mild temperature and pressure conditions. Carbon dioxide reduction is at the core of natural photosynthesis, and understanding the science and technology of this reaction is also central to society's efforts to mitigate carbon dioxide emission. It is an enormous challenge, but just the sort of problem that is worthy of sustained scientific investment. We are excited for the work ahead."

In its first five years of research, JCAP has made significant advances in a number of areas, including the automated and rapid discovery and characterization of new catalysts and light absorbers, the development of techniques for protecting the light-absorbing components in solar-fuels generators, and the creation of experimental protocols for objective evaluations of the activity and stability of materials. All of these technologies are critical to the development of solar-driven water splitting and the reduction of carbon dioxide to produce fuel.

For more information about JCAP, please visit http://solarfuelshub.org/.

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Tuesday, May 19, 2015
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Science in a Small World - Short Talks

Tuesday, May 19, 2015
Dabney Hall, Garden of the Associates – The Garden of the Associates

Science in a Small World - Poster Session #2

Tuesday, May 19, 2015
Dabney Hall, Garden of the Associates – The Garden of the Associates

Science in a Small World - Poster Session #1

Five from Caltech Elected to American Academy of Arts and Sciences

The American Academy of Arts and Sciences has elected five Caltech community members as academy fellows. They are faculty members Michael B. Elowitz, professor of biology and bioengineering and an investigator with the Howard Hughes Medical Institute; Mory Gharib (PhD '83), Hans W. Liepmann Professor of Aeronautics and Bioinspired Engineering, director of the Ronald and Maxine Linde Institute of Economic and Management Sciences, and vice provost; and Linda C. Hsieh-Wilson, professor of chemistry; and Caltech trustees James Rothenberg and Maria Hummer-Tuttle. The American Academy is one of the nation's oldest honorary societies. Members are accomplished scholars and leaders representing diverse fields including academia, business, public affairs, the humanities, and the arts.

 

Michael B. Elowitz was noted for his work that "helped to initiate synthetic biology." Elowitz studies genetic circuits—interacting genes and proteins that enable cells to sense environmental conditions and to communicate. He and his group build simplified synthetic genetic circuits and study their effects in bacteria, yeast, and mammalian cells. He has received numerous honors in recognition of his work, including a MacArthur Fellowship in 2007.
 

Mory Gharib and his group use nature's own design principles—apparent in fins, wings, blood vessels, and more—as inspiration for a myriad of inventions. They have studied fluid flows inside the zebrafish heart to develop efficient micropumps and more efficient artificial heart valves, and cactus spine to develop arrays of nanoneedles, based on carbon nanotubes, for painless drug delivery. Gharib holds nearly 100 patents, and was elected to the National Academy of Engineering in 2015.

Linda C. Hsieh-Wilson was noted for her pioneering work in the new fields of chemical glycobiology and chemical neurobiology. Her work combines organic chemistry and neurobiology in order to understand how carbohydrates contribute to fundamental brain processes such as cell growth and neuronal communication, neural development, and memory at the molecular level. She and her group discovered a means for suppressing tumor-cell growth by blocking the attachment of certain sugars to proteins, restricting delivery of certain carbohydrates to proteins within the tumor.

Maria Hummer-Tuttle, a lawyer, was a partner and chair of the management committee and co–managing partner of Manatt, Phelps and Phillips in Los Angeles. She currently serves on the boards of Caltech, the J. Paul Getty Trust, the W. M. Keck Foundation, the Suu Foundation, and the Foundation for Art and Preservation in Embassies. Hummer-Tuttle is president of the Hummer Tuttle Foundation, serves on the advisory board of the USC Center on Public Diplomacy at the Annenberg School as well as on the program advisory committee of the Annenberg Retreat at Sunnylands, and is a member of the Pacific Council on International Policy, the Council on Foreign Relations, and the Getty Conservation Institute Council.

Jim Rothenberg is chairman of the Capital Group Companies, Inc. In addition to his service on the Caltech board, he serves on the boards of Capital Research and Management Company, the Capital Group Companies, Inc., and American Funds Distributors, Inc. In addition, he is a portfolio counselor for the Growth Fund of America, as well as vice chairman of the Growth Fund of America and Fundamental Investors. A chartered financial analyst, he was named to the Harvard Corporation as the treasurer of Harvard University in 2004. He also serves as a director of Huntington Memorial Hospital in Pasadena.

Elowitz, Gharib, and Hsieh-Wilson join 83 current Caltech faculty as members of the American Academy. Also included in this year's list are five alumni: Robert Cohen (MS '70, PhD '72), St. Laurent Professor of Chemical Engineering at MIT and codirector of the DuPont-MIT Alliance; Alexei Filippenko (PhD '84), professor of astronomy at UC Berkeley; Katherine Hayles (MS '69), professor of literature at Duke University; Michael Snyder (PhD'83), professor and chair of genetics at Stanford University; and Donald Truhlar (PhD '70), professor of chemistry at the University of Minnesota.

Founded in 1780 by John Adams, James Bowdoin, John Hancock, and other scholar-patriots, the academy aims to serve the nation by cultivating "every art and science which may tend to advance the interest, honor, dignity, and happiness of a free, independent, and virtuous people." The academy has elected as fellows and foreign honorary members "leading thinkers and doers" from each generation, including George Washington and Ben Franklin in the 18th century, Daniel Webster and Ralph Waldo Emerson in the 19th, and Albert Einstein and Woodrow Wilson in the 20th.

A full list of new members is available on the academy website at https://www.amacad.org/content/members/members.aspx.

The new class will be inducted at a ceremony on October 10, 2015, in Cambridge, Massachusetts.

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