How do proteins molecules work? That was the question Rufus Worth Lumry II was determined to answer. And he did.
Surrounded by piles of paper and overflowing bookshelves in a tiny office in the basement of Smith Hall at the University of Minnesota, the beloved chemistry professor spent his 50-year career studying the subject, and along the way conducted landmark research to explain how protein molecules work.
“He was passionate about science,” said George Barany, a University of Minnesota chemistry professor and Rufus’ longtime colleague. “His research made people think. He was very inspiring.”
Lumry had been living at the Kenwood Senior Residence in Minneapolis until he died Saturday following a long illness. He was 92.
Lumry’s quest to crack the protein puzzle took root at Harvard University where the native of Bismarck, N.D., earned an undergraduate degree in chemistry, a master’s degree in physics and a doctoral degree in chemical physics. He spent two years at the University of Utah on a fellowship from the Merck & Co. paid through the National Research Council before he arrived at the University of Minnesota.
During his tenure at the U from 1953 to ’91, he wrote more than 130 papers on protein function, taught freshman chemistry and supervised more than 14 Ph.D. students. He mentored Nobel Prize winners, too. But he spent most of his time dedicated to research, an endeavor he continued in retirement as professor emeritus from 1991 to 2003. He published one of his most challenging papers on protein substructures in 2003, said Andreas Rosenberg, a retired University of Minnesota biochemistry professor.
“He was proud of his research,” said his son, Stephen, of Bellevue, Wash. “He always thought he was on the right track even though some people thought he was too far ahead of others.”
In 1990, the Laboratory for Biophysical Chemistry held a symposium in Kansas City, Mo., in Lumry’s honor. Called “The Thermodynamic Basis of Protein Structure and Function,” the event drew top researchers from around the world.
“It is difficult to summarize the broad range of Rufus Lumry’s many contributions to the understanding of protein function,” the publicity materials said. “It is the novelty and intuitive insight of his ideas and concepts which have been most valuable, many of which are provocative and controversial. He has had an important impact on the development of biophysical chemistry, and it is fitting to acknowledge his contributions with a symposium on the topic to which he has been so closely associated.”
Lumry was hardly the stodgy professor and researcher. He dressed flamboyantly, replete with plaid jackets, bow ties and argyle socks. He had a gregarious personality to match, his son said. Members of the Lumry Lunch Group, composed of former chemistry students and colleagues, recall his humor, kindness and devotion to his work.
Minnesota Monthly featured him in a column called “Eccentric Minnesotans” in its May 1997 edition.
“He was one of a kind,” Barany said.
In addition to his son, Stephen, Lumry is survived by another son, Rufus Worth Lumry III, of Bellevue, Wash.; a daughter, Ann Lumry, of St. Paul, five grandchildren and six great-grandchildren.
A memorial service will be held at 1:30 p.m. April 28 at the Campus Club at the Univeristy of Minnesota.