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Biochem grad inspired by Boiler footballIf you were to walk into a certain laboratory of the Swiss Federal Institute of Technology in Zurich, Switzerland, late on an autumn Saturday night, you might find a scientist and his team of researchers hard at work. Nothing unusual about that, until you notice that a computer is broadcasting the familiar sounds of a football game at Purdue’s Ross-Ade Stadium. Timothy Richmond (Biochemistry, ’70), known to scientists and biochemists around the world for his work in cellular structural biology and X-ray crystallography, is a Boilermaker fan from the days of Mike Phipps and Leroy Keyes. If you ask the man on the street what he thinks of when he imagines a world-famous biochemist (especially one who works at the renowned Eidgenoessische Technische Hochschule, Switzerland’s federal institute of technology), "football fan" probably isn’t going to be on the list. Biochemists’ minds thrill to metabolic cycles and transduction pathways, not pass routes and blocking schemes. But Richmond enjoys – and is inspired by – Purdue football, just as he enjoys applying the competitive nature of the sport to molecular biology. When Tim Richmond has been faced with seemingly insurmountable problems, he has found a way to come back and win, with a can-do drive that would bring a smile onto any football coach’s face. Richmond is so much a football fan that when the Purdue Department of Biochemistry invited him to return to campus for a few days this year to deliver the David W. Beach Memorial Lectureship, he picked a weekend in October that would allow him to also attend the Purdue-Michigan game. It was a good choice. That Saturday, Richmond watched the Boilermakers play the then-No. 6 ranked Michigan Wolverines for the Big Ten Conference lead and the inside track to the Rose Bowl. Purdue fell behind 21-3 in the first half, on the way to what looked like a Michigan rout. Purdue came back with a chance to win the game on a 32-yard field goal with just over two minutes remaining in the game, but the kick was wide to the left. But instead of giving up against what seemed to be an impossible situation, Purdue held its ground, and drove down the field for a second field goal with just four seconds remaining. This was the game winner, and Purdue went on to have its best season in 30 years. The game reminded some of Richmond’s own pursuit of excellence. Richmond grew up in Seattle and Philadelphia but decided to attend college at Purdue. During the second semester of his freshman year, Richmond decided to study biochemistry. He asked his adviser, Larry Butler, to help him get hands-on experience. He was quickly put to work in the laboratories of the Indiana State Seed Commissioner’s office. "I was impressed with the way the professors worked with me," Richmond says. "I had an awful lot of desire to succeed, but even given that, they still encouraged me constantly." During he next year Richmond decided he wanted to know more about the structure of the biological molecules he was working with. Purdue has one of the world’s leading laboratories that studies macromolecular biological structures, operated by Michael Rossmann, Purdue’s Hanley Distinguished Professor of Biological Sciences. It was there that Richmond was introduced to X-ray crystallography, a technique to determine the three-dimensional structure of a molecule by analyzing how X-rays bounce off crystals made up of the molecule. "From the beginning, Tim Richmond was always eager to understand everything he was doing, down to the last detail of the experimental procedure," Rossmann now says. "He has never changed, and as a result he has been highly successful in his very ambitious projects." Richmond’s research is on the structure and mechanics of DNA organization in living cells from yeast to man. How cells tightly but reversibly package their DNA is one of the marvels of the natural world. Each cell nucleus contains the equivalent of about a yard-long string of DNA. "There is so much DNA that it must have some interesting principles of packaging," Richmond says. "If you want to understand that, you need to see what it looks like." Richmond’s group solved the atomic structure of the nucleosome core particle, the fundamental repeating unit of chromatin that determines how genes are folded and plays a role in when they are turned on and turned off. Mark Hermodson, head of the Department of Biochemistry, says the nucleosome is an amazing, and complex, structure. "Inside a cell, DNA is wound like thread on spools so it can fit into a nucleus one millionth of a meter in diameter," Hermodson says. "But it has to be wound so the cell can retrieve the information in a single gene from the nucleus at the proper times in the life of the cell. This requires unwinding the spools, reading the information, then repackaging the gene, one of maybe 100,000 genes in a human cell." In 1984, while working at the MRC Laboratory of Molecular Biology in Cambridge, England, Richmond was able to describe the nucleosome structure at a resolution of 7 Angstrom (an Angstrom is one-billionth of a meter). But Richmond knew this resolution wasn’t good enough to allow him to view the DNA structure well enough to understand it. Rather than accept this as the final answer, Richmond decided to improve the quality of the crystals and devised a scheme to do it using new technologies. After moving to Zurich in 1987, it took his colleagues six years to successfully produce the new crystals. The nucleosome core structure was solved by X-ray crystallography in 1996 at the improved resolution of 2.8 Angstrom (and since, 1.9 Angstrom). "That was at the end of 1996, and we published the paper in 1997," Richmond says. "We patted each other on the back once or twice and went back to work." Others in the sciences weren’t so nonchalant about the research. "There have been two key structures of molecular complexes involved in expression of genes that have been solved in the past three years: the nucleosome core particle and the ribosome," Hermodson says. "Dr. Richmond's study of the nucleosome is a major advance in our understanding of how this complicated process occurs." Although Richmond receives professional awards and accolades now, he wasn’t always confident his research would be successful. When talking about his days of doubt, Richmond speaks as though he wasn’t there, even though he is talking about is own life. "One has a young family and nothing seems to be going very well," he says, carefully choosing his words. "People tell younger researchers that the problems they are working on are too big, that their plans are too ambitious. One can get worried about that." But Richmond knew his research was important for biologists and the medical advances that would arise from it. "I was silly, I guess, for taking on such a difficult problem" he says, laughing. "I like to study things that are at the center of what we need to know. If you want to have a deep understanding of themes central to biology, you need to know these things, and that is what has attracted me." Richmond compares the research process to a football player heading toward the goal line. "How do you keep going? You’ve got the ball and you’ve got to carry it to the end. You can’t stop and say, ‘I’m tired of this. This is as far as I go.’ Too much depends on it." It’s that sentiment that has propelled Richmond, and he says that he still draws encouragement from the Purdue community today. "It sounds terribly corny, but Purdue sports do inspire me. I know, when I listen to the games, that the Purdue teams are going to win. On Saturday against Michigan, I knew that they were going to win. They knew that they were going to win. It’s that attitude, that confidence, that carries you through." Contact Richmond atTimothy.Richamond@mol.biol.ethz.ch By Steve Tally Personal Profile: Tim RichmondOccupation: Biochemist Degree: BS (Biochem.) '70 Residence: Zurich, Switzerland Tim Richmond has many interests in addition to biochemistry and football. We asked him to list his five favorite sites on the Web: 1. ETH Biology Department home page 2. Protein Data Bank site for X-ray crystallography and NMR |