Caltech Named World's Top University in Times Higher Education Global Ranking

For the third year in a row, the California Institute of Technology has been rated the world's number one university in the Times Higher Education global ranking of the top 200 universities.

Harvard University, Oxford University, Stanford University, and the Massachusetts Institute of Technology round out the top five schools in the 2013–2014 rankings.

Times Higher Education compiled the listing using the same methodology as in the 2011–2012 and 2012–2013 surveys. Thirteen performance indicators representing research (worth 30 percent of a school's overall ranking score), teaching (30 percent), citations (30 percent), international outlook (which includes the total numbers of international students and faculty and the ratio of scholarly papers with international collaborators, 7.5 percent), and industry income (a measure of innovation, 2.5 percent) make up the data. The data were collected, analyzed, and verified by Thomson Reuters.

The Times Higher Education site has the full list of the world's top 400 schools and all of the performance indicators.

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Kathy Svitil
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Friday, October 4, 2013

Undergraduate Teaching Assistant Orientation

Caltech Researchers Synthesize Catalyst Important In Nitrogen Fixation

Inspired by an enzyme in soil microorganisms, researchers develop first synthetic iron-based catalyst for the conversion of nitrogen to ammonia.

As farming strategies have evolved to provide food for the world's growing population, the manufacture of nitrogen fertilizers through the conversion of atmospheric nitrogen to ammonia has taken on increased importance.

The industrial technique used to make these fertilizers employs a chemical reaction that mirrors that of a natural process—nitrogen fixation. Unfortunately, vast amounts of energy, in the form of high heat and pressure, are required to drive the reaction. Now, inspired by the natural processes that take place in nitrogen-fixing microorganisms, researchers at Caltech have synthesized an iron-based catalyst that allows for nitrogen fixation under much milder conditions.

In the early 20th century, scientists discovered a way to artificially produce ammonia for the manufacture of commercial fertilizers, through a nitrogen fixation technique called the Haber-Bosch process. Today, this process is used industrially to produce more than 130 million tons of ammonia annually. Microorganisms in the soil that live near the roots of certain plants can produce a similar amount of ammonia each year—but instead of using high heat and pressure, they benefit from enzyme catalysts, called nitrogenases, that convert nitrogen from the air into ammonia at room temperature and atmospheric pressure.

In work described in the September 5 issue of Nature, Caltech graduate students John Anderson and Jon Rittle, under the supervision of their research adviser Jonas Peters, Bren Professor of Chemistry and executive officer for chemistry, have developed the first molecular iron complex that catalyzes nitrogen fixation, modeling the natural enzymes found in nitrogen-fixing soil organisms. The research may eventually lead to the development of more environmentally friendly methods of ammonia production.

Natural nitrogenase enzymes, which prime inert atmospheric nitrogen for fixation through the addition of electrons and protons, generally contain two metals, molybdenum and iron. Over decades of research, this duality has caused a number of debates about which metal was actually responsible for nitrogenase's catalytic activity. Since a few research groups had modest success in synthesizing molybdenum-based molecular catalysts, many in the field believed that the debate had been settled. The discovery by Peters' group that synthetic iron complexes are also capable of this type of catalytic activity will reopen the discussion.

This finding, along with a wealth of data from structural biologists, biochemists, and spectroscopists, suggests that it may be iron—and not molybdenum—that is the key player in the nitrogen fixation in natural enzymes. The iron catalyst discovered by Peters and his colleagues may also help unravel the mystery of how these enzymes perform this reaction at the molecular level.

"We've pursued this type of synthetic iron catalyst for about a decade, and have banged our heads against plenty of walls in the process. So have a lot of other very talented folks in my field, and some for much longer than a decade," Peters says.

The finding is a first for the field, but Peters says that their current iron-based catalyst has limitations—the Haber-Bosch process is still the industrial standard. "Now that we finally have an example that actually works, everyone wants to know: 'Can it be used to make ammonia more efficiently?' The simple answer, for now, is no. While we're delighted to finally have our hands on an iron fixation catalyst, it's pretty inefficient and dies quickly. But," he adds, "this catalyst is a really important advance for us; there is so much we will now be able to learn from it that we couldn't before."

Funding for the research outlined in the Nature paper, titled "Catalytic conversion of nitrogen to ammonia by an iron model complex," was provided by the National Institutes of Health and the Gordon and Betty Moore Foundation.

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Arnold Appointed New Director of Rosen Bioengineering Center

Now in its sixth year of exploring the intersection between biology and engineering, the Donna and Benjamin M. Rosen Bioengineering Center has chosen Caltech professor Frances Arnold as its new director. Arnold, the Dick and Barbara Dickinson Professor of Chemical Engineering, Bioengineering and Biochemistry began her tenure as director on June 1.

A recipient of the 2011 National Medal of Technology and Innovation, Arnold pioneered methods of "directed evolution" – processes now widely used to create biological catalysts that are important in the production of fuels from renewable resources. She was selected for the directorship because "of her demonstrated leadership in the field of bioengineering," says Stephen Mayo, William K. Bowes Jr. Foundation Chair of the Division of Biology and Biological Engineering.

The Rosen Center supports bioengineering research through the funding of fellows and faculty from many disciplines, including applied physics, chemical engineering, synthetic biology, and computer science.

"Bioengineering is an incredibly exciting field right now," Arnold says. "Solutions to some of the biggest problems in science, medicine, and sustainability will come from the interface between biology and engineering, and Caltech is well positioned to be at the forefront. The Rosen Center will help make that happen with innovative programs for bioengineering research and education."

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Tom Miller Wins Teacher-Scholar Award

The Camille and Henry Dreyfus Foundation has recognized Thomas F. Miller, professor of chemistry at the California Institute of Technology (Caltech), with a 2013 Camille Dreyfus Teacher-Scholar Award.

The award provides a $75,000 unrestricted research grant to "support the research and teaching careers of talented young faculty in the chemical sciences," according to the foundation.

"I am very grateful to my colleagues in the Chemistry and Chemical Engineering Division here at Caltech for nominating me for this award," Miller says. "I am also thankful to the Dreyfus Foundation for its generous grant, which will greatly benefit my research efforts."

Miller is an expert in developing theoretical and computational methods to understand a variety of molecular processes including enzyme catalysis, solar energy conversion, dendrite formation in lithium batteries, and the transport of proteins across cell membranes.

The Camille Dreyfus Teacher-Scholar Awards program is open to institutions in the United States that offer a bachelor's degree or higher in the chemical sciences, biochemistry, materials chemistry, and chemical engineering. Academic institutions may nominate one researcher per year for the award.

Miller earned a bachelor of science degree from Texas A&M University in 2000 and a PhD at the University of Oxford in 2005. He became an assistant professor at Caltech in 2008 and in 2013 was named professor of chemistry. He is the recipient of a Dreyfus New Faculty Award, Sloan Research Fellowship, National Science Foundation CAREER Award, American Chemical Society Hewlett-Packard Outstanding Junior Faculty Award, and an Associated Students of Caltech Teaching Award.

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John D. Roberts Awarded AIC Gold Medal

John D. Roberts, Institute Professor of Chemistry, Emeritus, at the California Institute of Technology (Caltech) received the 2013 American Institute of Chemists Gold Medal. The AIC awarded the medal to Roberts at the Heritage Day event in April in Philadelphia hosted by its awarding partner, the Chemical Heritage Foundation (CHF).

The AIC established the Gold Medal, its highest award, in 1926 to recognize service to the science of chemistry and to the profession of chemist and chemical engineer in the United States. The Gold Medal has been presented jointly by the AIC and the CHF since 2003.

"I am very honored to have been selected to receive the American Institute of Chemists Gold Medal," Roberts says. "Throughout my career, I have been fortunate in being able to collaborate with the world's leading researchers, study and teach in highly respected institutions, and participate in some of the most important scientific discoveries since the middle of the 20th century."

Roberts is an expert on the leading research into the mechanisms of organic reactions, the chemistry of small ring compounds, and applications of nuclear magnetic resonance (NMR) spectroscopy to organic chemistry and biochemistry. He serves on the boards of directors of Organic Syntheses Inc. and University Science Books, and was a consultant to DuPont from 1950 to 2008.

Roberts received his Ph.D. in chemistry from UCLA in 1944. Following a period as an instructor in chemistry there, Roberts was awarded a National Research Council Fellowship at Harvard University in 1945. He joined the staff of the Massachusetts Institute of Technology (MIT) in 1946, becoming an associate professor by 1950. In 1953, Roberts became a professor of organic chemistry at Caltech. In 1972, he was appointed Institute Professor of Chemistry and in 1988, Institute Professor of Chemistry, Emeritus and Lecturer. From 1980 to 1983 he served Caltech as vice president, provost, and dean of the faculty.

In addition to his many scientific achievements and chemistry lab discoveries, Roberts also was responsible for breaking the longstanding gender barrier at Caltech by sponsoring Dorothy Semenow (PhD '55) to become the Institute's first female doctoral candidate in 1953. Bringing Semenow from MIT to study at Caltech is "clearly the best thing I have done at Caltech in the 60 years I have been here," he says.

Roberts is a recipient of the American Chemical Society Award in Pure Chemistry (1954), the Priestley Medal (1987), the National Medal of Science and  the Welch Award in Chemistry (both in 1990), the Glenn T. Seaborg Medal (1991), the Chemical Pioneer Award of the American Institute of Chemists and the Arthur C. Cope Award of the American Chemical Society (both in 1994), the National Academy of Sciences Award in Chemical Sciences (1999), and the National Academy of Sciences Award for Chemistry in Service to Society (2009).

In 1998, Chemical & Chemical Engineering News named him as one of the 75 most influential chemists in the last 75 years. In 2008, he was elected Fellow of the Royal Society of Chemistry and in 2009, Fellow of the American Chemical Society. He is a member of the American Chemical Society, the American Academy of Arts and Sciences, the American Philosophical Society, and the National Academy of Sciences.

Roberts is the author, with M. C. Caserio, of Basic Principles of Organic Chemistry (1965 and 1977 editions) and has written other textbooks on NMR and Hückel molecular orbital calculations, and more than 500 scientific papers. ACS Books published his autobiography, The Right Place at the Right Time, in 1990.

The AIC is a professional organization dedicated to fostering the advancement of the chemical profession in the United States. Previous AIC Gold Medalists include Alfred Bader, Arnold O. Beckman, Paul Berg, Elizabeth Blackburn, Herbert C. Brown, F. Albert Cotton, Carl Djerassi, Walter Gilbert, Harry B. Gray, Ralph F. Hirschmann, Roald Hoffmann, Robert L. McNeil, Jr., Glenn T. Seaborg, Oliver Smithies, Max Tishler, and George M. Whitesides.

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Thursday, September 26, 2013

Graduate TA Orientation & Teaching Conference

Caltech Seniors Receive Fulbright Fellowships

Three graduating Caltech seniors, Alex Wang, Joy Xie, and Philip Kong, have been selected to receive 2013–2014 Fulbright scholarships to pursue graduate studies abroad.

The Fulbright Program is the U.S. government's premier scholarship program. Set up by Congress in 1946 to foster mutual understanding among nations through educational and cultural exchanges, Fulbright grants enable U.S. students and artists to benefit from unique resources in every corner of the world. Each year more than 800 Americans study or conduct research in more than 140 nations through the Fulbright Program.

"It was a pleasure to work with these students," says Lauren Stolper, director of Fellowships Advising and Study Abroad and Caltech's Fulbright Program advisor. "They each had a well-thought-out research idea based at a host university abroad that will provide the resources and supervision needed to ensure a successful outcome. Our Fulbright Scholars are excellent representatives for the Institute as well as for the U.S.—and part of their role as a Fulbright Scholar is an ambassadorial one."

 

Chemical engineering major Alex Wang, from Dallas, Texas, will be spending a year at Imperial College London in the laboratory of professor Molly Stevens, who specializes in biomedical materials and their application to regenerative medicine. "My topic of study will be how the external stem-cell environment may be able to influence stem-cell behavior and differentiation," Wang says. In particular, he says, "I would be looking at the influence of the protein laminin on differentiation within an artificial hydrogel scaffold. This way, we can look at how these cells can potentially be better controlled in vitro. I chose this topic due to its potential applications in medicine, as well as the opportunity to apply the engineering principles I have learned at Caltech.

"I always wanted to see the UK and experience a brand new culture for an extended period of time. I have never been to Europe," he adds, "so this should be a very eye-opening experience. I am very thankful that Fulbright has given me this honor."

Upon his return, Wang will attend graduate school at MIT, studying biological engineering.

 

Joy Xie, a chemical engineering major from Troy, Michigan, will travel to Switzerland for a research project in bioengineering and protein chemistry, working with Jeffrey Hubbell at the École Polytechnique Fédérale de Lausanne.

"Hubbell has done some very translational work in tissue engineering and drug delivery," Xie explains. The goal of her project is to create protein therapeutics that can be used to induce immune tolerance to certain antigens, such as self-antigens, to help treat autoimmune diseases. "I picked this project because I have always been interested in medicine and how it is possible to combine knowledge from several different fields to create something that has the potential to be used in the medical industry," she says.

"Switzerland seems like an incredibly scenic and exciting place, and I have always wanted to visit it," adds Xie, who will attend Northwestern University to study chemical and biological engineering upon her return to the States. "I'm really grateful for this opportunity and excited to be able to be abroad!"

 

Philip Kong, a biology major from Philadelphia, will be headed this summer to Seoul National University in South Korea to work with professor Sunyoung Kim. Kong, who has been doing immunology research in David Baltimore's lab for the past two years, will be studying how to identify medically meaningful bioactive compounds used in Korea's traditional botanical medicines, with a particular emphasis on screening for activities that control the Th1 and Th2 pathways of the human immune system. Various immune diseases, such as rheumatoid arthritis and allergic diseases, will be considered in the work. "I wanted to try a different type of research than my undergraduate research had been. My new project gives me more opportunity to gain access to patient samples and have more immediate impact when it comes to treating autoimmune diseases like rheumatoid arthritis," says Kong, who plans to go to medical school to pursue an MD/PhD after his year abroad.

"There are many reasons why I wanted to go to Korea," he says, "but the main reason had to do with my project, which involves data from herbal medicine. South Korea is one of the two or three places where the practice of botanical medicine has a rich database regarding botanical medicines, including literature hundreds of years old with lists of plants and their clinical effects and safety profiles. In addition, only specific plants grow in South Korea due to the unique climate of the peninsula."

The Fulbright Program, Kong says, is an "exciting opportunity, and I feel that everyone at Caltech at least deserves a chance to study abroad and enjoy the new air of a different country. Any future Fulbright applicants should not hesitate to contact me if they would like to know more about the program."

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Kathy Svitil
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Frances Arnold Wins Eni Award for Renewable-Energy Work

PASADENA, Calif.—For the second year in a row, a faculty member from the California Institute of Technology (Caltech) has been awarded the Eni Award in Renewable and Non-Conventional Energy. This year, chemical engineer Frances Arnold—who pioneered methods of "directed evolution" for the production and optimization of biological catalysts—has been chosen to receive the distinction, along with her colleague James Liao of UCLA.

Arnold, Caltech's Dick and Barbara Dickinson Professor of Chemical Engineering, Bioengineering and Biochemistry, has shown that mimicking Darwinian evolution in the laboratory is an efficient way to engineer the amino-acid sequence of a protein, endowing it with new capabilities or improving its performance. Arnold and her colleagues have used directed evolution to improve catalysts for making fuels and chemicals from renewable resources.

"There are a lot of creative people working on renewable and non-conventional energy, so it is a huge honor to be selected for this distinction," Arnold says. "This prize recognizes the basic technology we've developed over the years, but especially the application of directed evolution to making things that we currently get from non-renewable hydrocarbons."

The Eni Awards are international prizes that recognize outstanding research and development in the fields of energy and the environment. Eni is an integrated energy company based in Italy. According to the company's website, "The Eni Award was created to develop better use of renewable energy, promote environmental research and encourage new generations of researchers."

A 24-person scientific award committee selects the honorees each year in four categories: New Frontiers of Hydrocarbons, Renewable and Non-Conventional Energy, Protection of the Environment, and Debut in Research. Three additional prizes are awarded for innovative and applied research within Eni, in energy and the environment.

In 2012, Harry A. Atwater, Caltech's Howard Hughes Professor and professor of applied physics and materials science, and director of the Resnick Sustainability Institute, along with his colleague Albert Polman of the Dutch Research Institute AMOLF, was awarded the same Eni Award in Renewable and Non-Conventional Energy, for developing new ultrathin, high-efficiency solar cells.

Of Caltech's back-to-back Eni Awards, Arnold says, "It shows that the renewable-energy research going on at Caltech is world-class. Other places may have much bigger programs, but for impact and accomplishment, the research that the Resnick Institute supports is recognized throughout the world as being at the very top. These groups are making real progress on some of the most important problems we face today."

Arnold, Liao, and the other 2013 awardees will receive their prizes on June 27 at the Presidential Palace in Rome.

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Kimm Fesenmaier
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Decision Making and Quality Control in Early Moments of a Protein’s Life

Watson Lecture Preview

Professor of Chemistry Shu-ou Shan studies the gears and springs in the molecular machinery of life. She'll be giving us a guided tour of the cellular assembly line at 8 p.m. on Wednesday, May 22, 2013 in Caltech's Beckman Auditorium. Admission is free.

 

Q: What do you do?

A: I'm a biochemist-slash-biophysicist. I want to understand how our cells' molecular machinery works. These machines are large assemblies of proteins and other molecules that fit together in very specific ways and whose parts move in close coordination to perform the functions of life. I'm particularly interested in understanding how these machines make accurate decisions in the crowded, complex environment inside the cell. These decisions ultimately control what the cell does—will it function correctly, will it turn into a cancer cell, or will it die prematurely?

I'm looking specifically at the decisions that have to be made by various cellular machines every time a new protein molecule is synthesized. For example, there are chaperone machines that help the new protein fold into the right structure. There are protein localizer machines that take the new protein to the right part of the cell—to an organelle, to the cell membrane, or even across the cell membrane, if the protein is a hormone or some other substance the cell intends to secrete. And there are all kinds of enzymes that put chemical tags on the new protein for all sorts of reasons.

We study how these machines work by using a lot of methods developed by chemists and physicists. For example, we can make a protein in a test tube and attach fluorescent dyes to various parts of it. The light from the fluorescence tells us how the protein is interacting with other proteins and how the protein's molecular structure is changing during those interactions. This lets us identify the important interactions that enable the protein to function properly. We do this over and over, putting the dyes in different places and using the data to build a model of how we think the protein works. Then we wipe away the crucial interactions by modifying the protein and see if that disrupts the protein's function in the cell in the ways we predicted.

 

Q: How did you get started on this line of work?

A: I've always believed that when true understanding comes, complexity reduces to simplicity. So the question for me when I was going through middle school and high school was, "What can I do to contribute to that enterprise?"

Then, in high school, I had a revelation. My biology class was studying Mendelian genetics, which are patterns of heredity that you can explain by recombining genes in different ways. Meanwhile, my organic chemistry class was learning about proteins and nucleic acids, and how a few simple principles of base pairing in a molecule of DNA led to a model for how our genetic information is replicated. And I made the connection that all the phenomena of heredity came down to chemical structures I could draw on a piece of paper. They happened because of changing chemical structures, which happened because chemical bonds were made or broken, which happened because the laws of physics drove them. That was an exciting moment.

I majored in chemistry and biochemistry at the University of Maryland, where I also took all the advanced math and physics classes available. They were not required, but I found them very interesting. I went to Stanford for my PhD, where I joined a lab that was trying to find the fundamental principles that explain how enzymes work. It was fantastic training, because we had to think very rigorously in terms of physics and chemistry while still trying to understand the connection to biological function. And at the end, I realized that I still wanted to do biology, so I went on to be a postdoc at a cell biology lab at UC San Francisco. That's where I started working on how proteins make decisions.

 

Q: What gets you really excited about it?

A: Being able to explain very complex and amazing phenomena in the cell at the level of chemical principles. We make a measurement of a molecular action in a test tube and put together a mathematical model that predicts how a certain protein is going to be treated by the cell. Then we go back and test those predictions, see if they match up—not just the trend of the line, but the actual numbers. Those are the divine moments when we really understand something.

My interest in science started with physics and chemistry. Like most physicists, I'm amazed by the beauty and elegance with which the laws of physics explain, and even predict, the phenomena we see around us. I still hold the optimistic belief that ultimately we will explain the complex phenomena of life in terms of simple principles. I guess if science is likened to a craft, I am really a watchmaker. I have to take it down to the very last detail and see how it's all pieced together.

 

Named for the late Caltech professor Earnest C. Watson, who founded the series in 1922, the Watson Lectures present Caltech and JPL researchers describing their work to the public. Many past Watson Lectures are available online at Caltech's iTunes U site.

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