Caltech Chemical Biologist SpecializingIn Brain Chemistry Named HHMI Investigator

PASADENA, Calif.--California Institute of Technology chemical biologist Linda Hsieh-Wilson has been named one of this year's new Howard Hughes Medical Institute Investigators. Hsieh-Wilson's research integrates chemistry and neurobiology to understand how the cells of the brain communicate with one another.

Hsieh-Wilson, an assistant professor of chemistry at Caltech, joins 42 other American researchers in the new coterie of HHMI Investigators. The prestigious grant is presented to researchers who have shown particularly high promise in their first four to 10 years as independent scientists.

"These scientists are on the rapidly rising slope of their careers and have made surprising discoveries in a short period of time," says Thomas R. Cech, the president of HHMI. "We have every reason to believe that they will use their creativity to extend the boundaries of scientific knowledge for many years to come."

For Hsieh-Wilson, a major focus of her research is to understand how the structure of carbohydrates and other molecules impacts the function of proteins in the brain. In so doing, she is breaking down boundaries between fields and extending an understanding of how the brain works at the molecular and even atomic level.

"The HHMI award gives us greater freedom and flexibility," says Hsieh-Wilson, who arrived at Caltech four and a half years ago. " We can take risks, explore new areas, and take our science to the next level."

The HHMI's biography of Hsieh-Wilson sums up her current research as the quest to discover how "the right chemistry keeps the brain working properly." To investigate the role of carbohydrates on proteins, for example, she has created new chemical tools for studying a chemical process known as glycosylation, which is thought to be important for functions such as learning, memory, and motor control. Hsieh-Wilson's research also has an important medical component in that she is studying how glycosylation may have a role in the molecular basis of diseases such as diabetes, Alzheimer's, and cancer.

Hsieh-Wilson is also the winner of an Alfred P. Sloan Research Fellowship, a Beckman Young Investigator Award, and a National Science Foundation Faculty Early Development (CAREER) Program award. A graduate of Yale with a bachelor's degree in chemistry, she earned her doctorate in bioorganic chemistry at UC Berkeley before joining Rockefeller University to do research in neurobiology.

The election of Hsieh-Wilson and Dianne Newman, Caltech's other new HHMI Investigator, brings the total number of HHMI Investigators in residence on campus to nine.

A nonprofit medical research organization, HHMI was established in 1953 by the aviator-industrialist Howard Hughes. The Institute, headquartered in Chevy Chase, Maryland, is one of the largest philanthropies in the world, with an endowment of $12.8 billion at the close of its 2004 fiscal year. HHMI spent $573 million in support of biomedical research and $80 million for support of a variety of science education and other grants programs in fiscal 2004.




Robert Tindol
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Toward a Longer, Healthier Life

PASADENA, Calif. - The Spanish explorer Ponce de Leon spent a fair amount of his time in 1513 looking for the fountain of youth. The upside was that he discovered Florida. The downside was that the fountain was a myth. Now in two separate awards from the Ellison Medical Foundation, two scientists from the California Institute of Technology are taking a much more scholarly approach to the ravages of aging. Harry Gray, a chemist, has been awarded $970,000 to reveal the structure of a protein and a peptide that underlie two age-related diseases, Alzheimer's and Parkinson's, while biologist Alexander Varshavsky has been awarded $972,000 to conduct a systematic investigation of the genetics and biochemistry of aging.

Gray, the Arnold O. Beckman Professor of Chemistry, notes that approximately one million Americans suffer from Parkinson's, while 4.5 million have Alzheimer's. In order to design a drug to combat these two diseases, a key step is to understand the critical structural differences between normal proteins and the malignant proteins that comprise these diseases.

Both Alzheimer's and Parkinson's are associated with the accumulation in the brain of aggregates of proteins known as fibrils. In Parkinson's, the fibrils are composed of the protein alpha-synuclein, while in Alzheimer's, the fibrils or plaques are composed of the AB amyloid peptide. Alpha-synuclein and AB amyloid peptide are known as "disordered biopolymers," meaning that they do not have well-defined structures. Because of this lack of structure, the traditional tools used by chemists, such as x-ray crystallography and nuclear magnetic resonance spectroscopy, are virtually useless. They are only effective if the peptides and proteins being studied have well-defined structures in crystals or solutions.

Instead, Gray and his colleagues plan to use laser spectroscopic methods developed in Caltech's Beckman Institute to gain new insights into the structures, dynamics, and misfolding of malignant proteins and peptides. One of the most powerful methods they will use will employ an ultrafast camera to obtain distances between atoms in disordered structures that are constantly changing.

"We're very excited about the possibility of applying our laser methods to study proteins and peptides that are involved in disease in older people," says Gray. "We have a chance to identify toxic species that lead to these diseases, and point the way to successful interventions."

For Alexander Varshavsky, the Howard and Gwen Laurie Smits Professor of Cell Biology, it is the causes and alterations of the aging process that interest him. Every cell contains within it a molecular machine to eventually destroy its own proteins, he notes. The mechanisms and functions of this so-called regulated protein degradation became (mostly) understood over the last 25 years, in large part through discoveries in Varshavsky's lab. When a protein called ubiquitin is linked to another protein in a cell, that protein is marked for destruction. The molecular machines inside a cell that link ubiquitin to other proteins, and the intracellular machinery that "recognizes" ubiquitin-linked proteins and destroys them, are elaborate and complex. "Detailed understanding of these protein-destruction pathways will have a profound impact on the practice of medicine," says Varshavsky, "because all kinds of things that go wrong with us, from cancer and infectious diseases, to neurodegenerative syndromes and even normal aging, have a lot to do with either inherent imperfections of the ubiquitin system, or with an overt damage to it in a specific disease." Many clinical drugs of the future, he notes, will be designed to suppress, enhance, or otherwise modify various aspects of the ubiquitin system.

In this research Varshavsky will overexpress, selectively and in a controlled manner, specific components of the mouse ubiquitin system in intact mice, in order to determine the effects of such alterations on the rate of aging. He also plans to use analogous approaches with a much simpler organism, S. cerevisiae, common baker's yeast. His aim is to discover the molecular circuits that contribute to normal aging, and also to see whether some of the alterations that he plans to introduce could slow down the aging process.

The Ellison Medical Foundation is a nonprofit corporation that was established by a gift from Mr. Lawrence J. Ellison to support basic biomedical research to understand aging processes and age-related diseases and disabilities. Through various award mechanisms, including the Senior Scholar and New Scholar award programs, the foundation fosters research by means of grants-in-aid to investigators at universities and laboratories within the United States.

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Systems Biology Could Augur New Age for Predictive and Preventive Medicine

PASADENA, Calif./SEATTLE--The dream of monitoring a patient's physical condition through blood testing has long been realized. But how about detecting diseases in their very early stages, or evaluating how they are responding to treatment, with no more to work with than a drop of blood?

That dream is closer to realization than many of us think, according to several leading experts advocating a new approach known as systems biology. Writing in the current issue of the journal Science, Institute for Systems Biology immunologist and technologist Leroy Hood and California Institute of Technology chemist Jim Heath and their colleagues explain how a new approach to the way that biological information is gathered and processed could soon lead to breakthroughs in the prevention and early treatment of a number of diseases.

The lead author of the Science article is Leroy Hood, a former Caltech professor and now the founding director of the Institute for Systems Biology in Seattle. According to Hood, the focus of medicine in the next few years will shift from treating disease--often after it has already seriously compromised the patient's health--to preventing it before it even sets in.

Hood explains that systems biology essentially analyzes a living organism as if it were an electronic circuit. This approach requires a gigantic amount of information to be collected and processed, including the sequence of the organism's genome, and the mRNAs and proteins that it generates. The object is to understand how all of these molecular components of the system are interrelated, and then predict how the mRNAs or proteins, for example, are affected by disturbances such as genetic mutations, infectious agents, or chemical carcinogens. Therefore, systems biology should be useful for diseases resulting from genetics as well as from the environment.

"Patients' individual genome sequences, or at least sections of them, may be part of their medical files, and routine blood tests will involve thousands of measurements to test for various diseases and genetic predispositions to other conditions," Hood says. "I'll guarantee you we'll see this predictive medicine in 10 years or so."

"In this paper, we first describe a predictive model of how a single-cell yeast organism works," Heath explains, adding that the model covers a metabolic process that utilizes copious amounts from data such as messenger RNA concentrations from all the yeast's 6,000 genes, protein-DNA interactions, and the like.

"The yeast model taught us many lessons for human disease," Heath says. "For example, when yeast is perturbed either genetically or through exposure to some molecule, the mRNAs and proteins that are generated by the yeast provide a fingerprint of the perturbation. In addition, many of those proteins are secreted. The lesson is that a disease, such as a very early-stage cancer, also triggers specific biological responses in people. Many of those responses lead to secreted proteins, and so the blood provides a powerful window for measuring the fingerprint of the early-stage disease."

Heath and his colleagues write in the Science article that, with a sufficient number of measurements, "one can presumably identify distinct patterns for each of the distinct types of a particular cancer, the various stages in the progression of each disease type, the partition of the disease into categories defined by critical therapeutic targets, and the measurement of how drugs alter the disease patterns. The key is that the more questions you want answered, the more measurements you need to make. It is the systems biology approach that defines what needs to be measured to answer the questions."

In other words, the systems biology approach should allow therapists to catch diseases much earlier and treat them much more effectively. "This allows you to imagine the pathway toward predictive medicine rather than reactive medicine, which is what we have now," Heath says.

About 100,000 measurements on yeast were required to construct a predictive network hypothesis. The authors write that 100,000,000 measurements do not yet enable such a hypothesis to be formulated for a human disease. In the conclusion of the Science article, the authors address the technologies that will be needed to fully realize the systems approach to medicine. Heath emphasizes that most of these technologies, ranging from microfluidics to nanotechnologies to molecular-imaging methods, have already been demonstrated, and some are already having a clinical impact. "It's not just a dream that we'll be diagnosing multiple diseases, including early stage detection, from a fingerprick of blood," Heath says.

"Early-stage versions of these technologies will be demonstrated very soon."

The other authors of the paper are Michael E. Phelps of the David Geffen School of Medicine at UCLA, and Biaoyang Lin of the Institute for Systems Biology.

Robert Tindol

Chemists at Caltech devise new, simpler wayto make carbohydrates

PASADENA, Calif.--Chemists at the California Institute of Technology have succeeded in devising a new method for building carbohydrate molecules in a simple and straightforward way that requires very few steps. The new synthesis strategy should be of benefit to scientists in the areas of chemistry and biology and in the pharmaceutical industry.

In an article published online August 12 by the journal Science on the Science Express Website, Caltech chemistry professor David MacMillan and his graduate student Alan Northrup describe their new method of making carbohydrates in two steps. This is a major improvement over current methods, which can require up to a dozen chemical steps.

"The issue with carbohydrate utilization is that, for the last 100 years, scientists have needed many chemical reactions to differentiate five of the six oxygen atoms present in the carbohydrate structure," explains MacMillan, a specialist in organic synthesis. "We simplified this to two steps by the invention of two new chemical reactions that are based on an old but powerful chemical transformation known as the aldol reaction. Furthermore, we have devised methods to selectively build oxygen differentiated glucose, mannose, or allose in just two chemical steps."

MacMillan has also demonstrated that this new method for carbohydrate synthesis allows easy access to unnatural carbohydrates for use in medicinal chemistry and glycobiology as well as in a number of diagnostic techniques. One application involves a rare form or carbon known as carbon-13, which is easier to identify with magnetism-based analytical methods.

By using the readily available and inexpensive 13C-labeled form of ethylene glycol, MacMillan and Northrup have been able to construct the all-13C-labeled versions of carbohydrates in only four chemical steps. For comparison, the previous total synthesis of this all-13C-labeled carbohydrate was accomplished in 44 chemical steps.

"Carbohydrates are essential to human biology, playing key roles in everything from our growth and development to our immune system and brain functions," says John Schwab, a chemist at the National Institute of General Medical Sciences, which supported the research. "They also play critical roles in plants, bacteria, and viruses, where they have huge implications for human health. But because they are so difficult to work with, carbohydrates are not nearly as well understood as DNA and proteins.

"MacMillan's technique will allow scientists to more easily synthesize and study carbohydrates, paving the way for a deeper understanding of these molecules, which in turn may lead to new classes of drugs and diagnostic tools," Schwab adds.

"One of the central goals of chemical synthesis is to design new ways to build molecules that will greatly benefit other scientific fields and ultimately society as a whole," MacMillan says. "We think that this new chemical sequence will help toward this goal; however, there is a bounty of new chemical reactions that are simply waiting to be discovered that will greatly impact many other areas of research in the biological and physical sciences."

The title of the paper is "Two Step Synthesis of Carbohydrates by Selective Aldol Reactions." The paper will be published in the journal Science at a later date.


New Class of Reagents Developed by Caltech Chemical Biologists for In Vivo Protein Tracking

PASADENA, Calif.--One of the big problems in biology is keeping track of the proteins a cell makes, without having to kill the cell. Now, researchers from the California Institute of Technology have developed a general approach that measures protein production in living cells.

Reporting in the July 26 issue of the journal Chemistry and Biology, Caltech chemistry professor Richard Roberts and his collaborators describe their new method for examining "protein expression in vivo that does not require transfection, radiolabeling, or the prior choice of a candidate gene." According to Roberts, this work should have great impact on both cell biology and the new field of proteomics, which is the study of all the proteins that act in living systems.

"This work is a result of chemical biology—chemists, and biologists working together to gain new insights into a huge variety of applications, including cancer research and drug discovery," says Roberts.

"Generally, there is a lack of methods to determine if proteins are made in response to some cellular stimuli and what those specific proteins are," Roberts says. "These are two absolutely critical questions, because the behavior of a living cell is due to the cast of protein characters that the cell makes."

Facing this problem, the Roberts team tried to envision new methods that would enable them to decipher both how much and what particular protein a cell chooses to make at any given time. They devised a plan to trick the normal cellular machinery into labeling each newly made protein with a fluorescent tag.

The result is that cells actively making protein glow brightly on a microscope slide, much like a luminescent Frisbee on a dark summer night. Importantly, these tools can also be used to determine which particular protein is being made, in much the same way that a bar code identifies items at a supermarket checkout stand.

To demonstrate this method, the team used mouse white blood cells that are very similar to cells in the human immune system. These cells could be tagged to glow various colors, and the tagged proteins later separated for identification.

Over the next decade, scientists hope to better understand the 30,000 to 40,000 different proteins inside human cells. The authors say they are hopeful that this new approach will provide critical information for achieving that goal.

The title of the paper is "A General Approach to Detect Protein Expression In Vivo Using Fluorescent Puromycin Conjugates." For more information, contact Heidi Hardman at

Robert Tindol

Zewail Named to TIAA-CREF Board of Trustees

PASADENA, Calif.— Ahmed H. Zewail, Nobel laureate and the Linus Pauling Professor of Chemical Physics and professor of physics at the California Institute of Technology, has been named to the board of trustees of TIAA-CREF (Teachers Insurance and Annuity Association-College Retirement Equities Fund).

CREF is an investment company within the TIAA-CREF group of companies and Zewail will serve on the CREF board joining seven other renowned economists and leaders in the education and finance sectors.

"As a scientist I feel I'm also a citizen of the world and should make every effort to help our society. TIAA-CREF is a special institution charting the future of education and educators and I will do my best to aid in this noble mission," said Zewail.

"We are honored and delighted that Ahmed Zewail has joined our Board of Trustees. As one of the world's most eminent scholars and researchers, he is superbly qualified to help us fulfill our commitment to institutions and individuals in the not-for-profit community who contribute so much to our society," said TIAA-CREF chairman, president and CEO Herb Allison.

TIAA-CREF is a national financial services leader and the premier retirement system for education and research employees. It has $307 billion in assets and 2.9 million retirement system participants within 15,000 participating institutions.

Jill Perry
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White House Names Three from Caltech Faculty as Presidential Early Career Award Winners

PASADENA, Calif.—Three members of the faculty at the California Institute of Technology have been named among the most recent winners of the prestigious Presidential Early Career Award for Scientists and Engineers (PECASE). The honor was announced today by the White House.

The three are Babak Hassibi, an electrical engineer who studies data transmission and wireless communications system; Mark Simons, a geophysicist who specializes in understanding the mechanical behavior of Earth using radar and other satellite observations of the motions of Earth's surface; and Brian Stoltz, an organic chemist who specializes in the synthesis of structurally complex, biologically active molecules.

Hassibi was cited by the White House for his "fundamental contributions to the theory and design of data transmission and reception schemes that will have a major impact on new generations of high-performance wireless communications systems. He has nurtured creativity in his undergraduate and graduate students by involving them in research and inspiring them to apply new approaches to communications problems."

An associate professor of electrical engineering at Caltech and a faculty member since 2001, Hassibi earned his bachelor's degree from the University of Tehran in 1989, and his master's and doctorate degrees from Stanford in 1993 and 1996, respctively. He is the holder or coholder of four patents for communications technology, and is the winner of several awards, including the 2002 National Science Foundation Career Award, the 1999 American Automatic Control Council O. Hugo Schuck Best Paper Award, the 2003 David and Lucille Packard Fellowship for Science and Engineering, and the 2002 Okawa Foundation Grant for Telecommunications and Information Sciences.

Simons, an associate professor of geophysics, combines satellite data with continuum mechanical models of Earth to study ongoing regional crustal dynamics, including volcanic and tectonic deformation in Iceland, crustal deformation and the seismic cycle in California, Chile, and Japan, and volcanic and tectonic deformation in and around Long Valley, California. He also uses the gravity fields of the terrestrial planets to study the large-scale geodynamics of mantle convection and its relationship to tectonics.

Simons earned his bachelor's degree at UCLA in 1989, and his doctorate from MIT in 1995. He was a postdoctoral scholar at Caltech for two years before joining the faculty in 1997.

Stoltz has been an assistant professor of chemistry at Caltech since 2000. He earned his bachelor's degree at Indiana University of Pennsylvania in 1993, his master's and doctorate degrees at Yale University in 1996 and 1997, respectively. Before joining the Caltech faculty he spent two years at Harvard University as a National Institutes of Health (NIH) Postdoctoral Fellow. His work is aimed at developing new strategies for creating complex molecules with interesting structural, biological, and physical properties. The goal is to use these complex molecules to guide the development of new reaction methodology to extend fundamental knowledge and to potentially lead to useful biological and medical applications.

Stoltz, an Alfred P. Sloan Fellow, is the recipient of a Research Corporation Cottrell Scholars Award, the Camille and Henry Dreyfus New Faculty Award, and the Pfizer Research Laboratories Creativity in Synthesis Award. Additionally, he was named as an Eli Lilly Grantee in 2003 and has won a number of young faculty awards from pharmaceutical companies such as Merck Research Laboratories, Abbott Laboratories, GlaxoSmithKline, Johnson & Johnson, Amgen, Boehringer Ingelheim, and Roche. At Caltech he won the 2001 Graduate Student Council Teaching Award and Graduate Student Council Mentoring Award.

The PECASE awards were created in 1996 by the Clinton Administration "to recognize some of the nation's most promising junior scientists and engineers and to maintain U.S. leadership across the frontiers of scientific research." The awards are made to those whose innovative work is expected to lead to future breakthroughs.



Robert Tindol
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Two Caltech Faculty Receive Franklin Medals

PASADENA—Two members of the California Institute of Technology faculty, chemist Harry Gray and biologist Seymour Benzer, are among this year's recipients of the prestigious Benjamin Franklin Medals.

The honor is bestowed annually by the Franklin Institute in Philadelphia to outstanding American scientists and technologists. Approaching its 180th anniversary, the Franklin Medal has been presented in the past to Albert Einstein, Samuel F. B. Morse, Alexander Graham Bell, Steven Hawking, Gordon Moore, Jane Goodall, and Noam Chomsky, among others. Past recipients have also won 103 Nobel Prizes through the years.

Gray, who is being recognized for his work in metalloproteins, is the Beckman Professor of Chemistry and founding director of the Beckman Institute at Caltech. A Caltech professor since 1966, he served as chair of the Division of Chemistry and Chemical Engineering from 1978 to 1984. He is a member of the National Academy of Sciences, received the National Medal of Science in 1986, and is also the recipient of the Wolf Prize and the Harvey Prize. Gray was named a foreign member of Great Britain's Royal Society, as well as a member of the American Philosophical Society.

Benzer is the Boswell Professor of Neuroscience, Emeritus, at Caltech, and a preeminent molecular biologist who has worked on phage genetics, nervous system development, and behavioral genetics of the fruit fly. He has been at Caltech since 1965. He is a member of the National Academy of Sciences. He received the National Medal of Science in 1983, and is also the recipient of the Lasker Award, the Wolf Prize, the Crafoord Prize, and the Harvey Prize. He is a member of the Royal Society and the American Philosophical Society.

Benzer and Gray will be honored in Philadelphia on April 29 at the annual Franklin Institute Awards Ceremony and Dinner, which is held in the Benjamin Franklin National Memorial.

Robert Tindol
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Revolutionary Chemical Instrument Receives Historical Recognition

PASADENA, Calif. -- In the mid-1930s, Arnold O. Beckman, then an assistant professor of chemistry at the California Institute of Technology, solved a problem confronting the California citrus industry: how to get a rapid and accurate measure of the acidity of lemon juice. His pH meter--a faster and simpler acid and alkaline measuring device--revolutionized instrumentation.

On Wednesday, March 24, the development of the Beckman pH meter will be designated a National Historic Chemical Landmark in a special ceremony at Caltech. The American Chemical Society, the world's largest scientific society, is sponsoring the landmark program. Charles P. Casey, president of the society, will present the bronze plaque to David A. Tirrell, chair of the division of chemistry and chemical engineering at Caltech.

The Beckman pH meter was the first commercially successful electronic pH meter. Beckman soon discovered there was a market for the instrument, which he manufactured on the side while he continued his academic career. Strong sales led Beckman to leave his teaching post in 1939 and devote his full attention to the company.

Beckman Instruments went on to become a leader in manufacturing instruments used in medicine, industry, and scientific research. Now called Beckman Coulter, it is a multinational company with sales in excess of $2 billion last year.

Later in his long life (he will be 104 in April), Beckman turned to philanthropy. The Arnold and Mabel Beckman Foundation--established in 1977--has donated more than $350 million to support scientific research and education. The foundation provides ongoing research support to five Beckman centers and institutions in the United States, including one at Caltech (which is in addition to numerous other generous gifts by the Arnold and Mabel Beckman Foundation to Caltech).

The American Chemical Society established the chemical landmarks program in 1992 to recognize seminal historic events in chemistry and increase public awareness of the contributions of chemistry to society. The program will begin at 2 p.m. in the Beckman Institute auditorium on the Caltech campus. Speakers include John D. Roberts, institute professor of chemistry, emeritus, Caltech; Gerald Gallwas, the Arnold and Mabel Beckman Foundation; Arnold Thackray, the Chemical Heritage Foundation; and Harry Gray, Arnold O. Beckman Professor of Chemistry and the founding director of the Beckman Institute.


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Professor Harry Gray Awarded Wolf Prize

PASADENA, Calif. — Harry Gray still recalls the day in 1982 when, after eight years of research, he and his colleagues finally proved that electrons can literally jump from one molecule to another. "I was ecstatic," recalls the California Institute of Technology chemist. "My whole group was ecstatic." Gray is referring to electron transfer (ET), the process of moving an electron from one place to another, which is critical for life.

For his insight into ET, Gray, the Arnold O. Beckman professor of chemistry and the founding director of the Beckman Institute at Caltech, has been awarded the 2004 Wolf Prize in Chemistry. Specifically, the Wolf foundation is honoring Gray for his "pioneering work in bio-inorganic chemistry, unraveling novel principles of structure and long-range electron transfer in proteins." The prize includes an honorarium of $100,000.

"It is really special to be recognized for experimental work that's been done with students and other good friends," says Gray. "It has been so much fun."

Electron-transfer reactions are ubiquitous in the chemistry of biological systems. They are a fundamental process that, among other functions, are responsible for the generation of energy in a cell.

Gray studies the tiny bits of inorganic material in living molecules, such as iron or copper, which, within proteins, have long been known to transfer electrons. But conventional wisdom held that in order for such exchanges to take place, the molecules had to be physically close enough to interact. The puzzle was how the few metal atoms in proteins, surrounded by thousands of other atoms, could maneuver close enough for the exchange. Further, in biological systems the timing always has to be perfect in order to allow for such things as breaking down food and generating energy, conducting photosynthesis, or fixing nitrogen.

The answer, Gray and his colleagues discovered, is that in biological systems, electrons really do jump, and jump big-his work shows that electrons can leap across at least 30 atoms in a large protein molecule in less than one millionth of a second.

His insights could have practical applications in a number of areas. Because ET plays a role in the body's natural barriers against foreign substances, his work may influence the design of drugs to get around these barriers. It also has implications for computer miniaturization, energy storage, and the effort to develop an artificial counterpart to photosynthesis. Gray, a Caltech professor since 1966, is the recipient of numerous distinguished honors and awards. These include the National Medal of Science in 1986 and six national awards from the American Chemical Society, including the Priestley Medal, the Society's highest honor. Last year he received both the National Academy of Sciences Award in Chemical Sciences and an honorary degree from the University of Copenhagen that included an audience with Queen Margrethe II of Denmark.

The Wolf Prize was established in 1978 and is designed to promote science and art for the benefit of mankind. In presenting him the prize, the foundation noted "his ingenious chemistry, meticulously executed, has given us a real understanding, for the first time, of a biological process of great significance for life."

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