| SUBJECT |
the process by which asparagine and glutamine amino acid side chains spontaneously shed their amide groups--has puzzled chemist Arthur B. Robinson for more than four decades. "Why would nature use two building blocks so fundamentally unstable to build proteins?" Robinson muses. "If these residues' inherent instabilities weren't useful to the cell in some way, they would've been eliminated long ago." HOT SPOTS Deamidation of two key asparagines (shown in red) in Bcl-xL prevents this protein from carrying out its normal function, to block cell suicide. COURTESY OF BENJAMIN DEVERMAN Robinson--the founder, director, and sole full-time scientist of the Oregon Institute of Science & Medicine, Cave Junction, Ore.--thinks asparagines and glutamines serve as molecular clocks that regulate protein turnover and cellular aging. He and others have provided experimental evidence linking the in vivo turnover rates of cytochrome c and rabbit muscle aldolase with these proteins' deamidation rates. But definitive proof of deamidation's physiological role has remained elusive, causing some to wonder if this modification is simply an interesting but unimportant anomaly. Research At Oregon Institute Is A Family Affair Twenty-some years ago, chemist Arthur B. Robinson founded the Oregon Institute of Science & Medicine (OISM), nestled on 300-plus acres of farmland in rural Cave Junction, Ore. The move to Cave Junction, located just miles from the California border, capped a turbulent time in Robinson's life. He and two-time Nobel Laureate Linus C. Pauling, his collaborator and friend, had quarreled over Robinson's contention that large doses of vitamin C, recommended by Pauling, caused tumors in mice. Robinson relocated to restart his career--and to regain his scientific independence. ALL IN THE FAMILY The Robinson children help out in the labs at the Oregon Institute of Science & Medicine. Noah has published several papers with his dad on protein deamidation. OISM PHOTO OISM's faculty boasts just a handful of other researchers, including Nobel Laureate R. Bruce Merrifield, an emeritus faculty member at Rockefeller University, New York City. But it's Robinson and his family who do the real research here. His six children, all of whom were homeschooled with a curriculum of Robinson's own design, grew up splitting their free time between farm chores and assisting their dad in the lab. This has resulted in a chemistry family. Robinson's eldest son, Zachary, 26, earned a B.S. in chemistry from Oregon State University and is now enrolled in both grad school in chemistry and a veterinary medicine program at Iowa State University. Noah, 24, earned his chemistry B.S. from Southern Oregon University, in Ashland, and is now a third-year grad student in chemistry at California Institute of Technology. Arynne, 23, is an undergraduate studying chemistry at Bethel College, St. Paul, Minn., and twins Joshua and Bethany, 21, are studying mathematics and chemistry, respectively, at Southern Oregon University. Matthew is just 15 and already showing strong interest in science, his dad says. Robinson's late wife, Laurelee, also had B.S. and M.S. degrees in chemistry. With a yearly research budget of merely $200,000 and a hand-me-down mass spectrometer as its most state-of-the-art instrument, this nonprofit research institute is a bare-bones operation. OISM accepts no government or industrial support, relying instead on private donations and income from sales of Robinson's homeschooling curriculum. Even so, this family effort has churned out a significant body of work. Robinson--who thinks that increased carbon dioxide levels may in fact have environmental benefit and who views global warming as a politically motivated myth--is studying the effect of high carbon dioxide levels on mice. He and his son Zachary gained notoriety when they initiated a 1998 petition drive against the Kyoto protocol. But Robinson's research interests remain centered on the impact of protein sequence and structure on the relative chemical stability of asparaginyl and glutaminyl residues in cellular proteins. Like other research at the institute, this is a family affair, with the elder Robinson and son Noah working hand-in-hand. In fact, Robinson says, "the key creative work on this project was done entirely by Noah." But his kids are getting older, and Robinson admits the family affair may not last forever. "Each of my children is quite accomplished--so I expect that OISM will soon need to compete for them with other institutions." |
| UPDATE | 02.2003 |
| AUTHOR | Arthur B. Robinson --the founder, director, and sole full-time scientist of the Oregon Institute of Science & Medicine, Cave Junction, Ore.-- |
| LITERATURE REF. | This data is not available for free |
|
Want more information ? Interested in the hidden information ? Click here and do your request. |