Charles Storrs

Charles Storrs. Charles Storrs was an American biochemist whose pioneering research into the mechanisms of protein folding and enzyme catalysis fundamentally reshaped modern molecular biology. His elegant experiments in the 1960s and 1970s provided the first rigorous kinetic framework for understanding how polypeptide chains achieve their functional three-dimensional structures, a problem central to cell biology and medicine. For these contributions, he was awarded the Nobel Prize in Chemistry in 1975, sharing the honor with colleagues William N. Lipscomb Jr. and John B. Fenn.

Early life and education

Born in Boston to a family with deep ties to New England academia, Storrs displayed an early aptitude for the natural sciences. He attended Phillips Academy in Andover before enrolling at Harvard University, where he earned an A.B. in chemistry in 1949 under the mentorship of future Nobel laureate Robert Burns Woodward. He then pursued graduate studies at the Massachusetts Institute of Technology (MIT), completing his Ph.D. in biochemistry in 1954. His doctoral thesis, supervised by John T. Edsall, investigated the physical chemistry of amino acids, laying the groundwork for his later research.

Career

Following his doctorate, Storrs conducted postdoctoral research at the University of Cambridge at the Medical Research Council Laboratory of Molecular Biology, a formative period where he collaborated with future Nobel laureates Max Perutz and John Kendrew. In 1957, he returned to the United States to join the faculty of Yale University as an assistant professor. He moved to Stanford University in 1963, where he spent the majority of his career, eventually chairing the Department of Biochemistry. Storrs also served as a visiting professor at the Weizmann Institute of Science in Israel and held advisory roles for the National Institutes of Health and the American Cancer Society.

Contributions to science

Storrs's most significant work centered on the protein folding problem. Utilizing the enzyme ribonuclease A as a model system, he and his team demonstrated that a denatured protein could spontaneously refold into its native, active conformation without external guidance, a discovery that overturned prevailing assumptions about cellular assembly. He developed novel techniques in stopped-flow kinetics and spectrophotometry to measure the rapid steps of folding intermediates. Furthermore, his research into allosteric regulation provided critical insights into how enzymes like aspartate transcarbamoylase are controlled, influencing fields from metabolic pathway analysis to pharmacology. His 1968 monograph, *Kinetics of Macromolecular Assembly*, became a standard text.

Personal life

Storrs married Eleanor Vance, a historian of Renaissance art, in 1956; they had three children. An avid alpinist, he was a member of the American Alpine Club and participated in expeditions to the Andes and the Himalayas. He was also a skilled cellist and performed with several community orchestras in the San Francisco Bay Area. Storrs was known for his modest demeanor and his dedication to mentoring students, many of whom, like Peter G. Wolynes, became leaders in biophysics and computational biology.

Legacy and honors

Charles Storrs's legacy is enshrined in the foundational principles of structural biology and biochemistry. The Storrs Lecture at Stanford University and the Storrs Award from the Protein Society are named in his honor. Beyond the Nobel Prize in Chemistry and the National Medal of Science, his accolades included the Gairdner Foundation International Award, the Linus Pauling Award, and election to the National Academy of Sciences, the American Academy of Arts and Sciences, and the Royal Society as a Foreign Member. His conceptual frameworks remain essential for understanding diseases like Alzheimer's disease and cystic fibrosis, which are linked to protein misfolding.

Category:American biochemists Category:Nobel laureates in Chemistry Category:1928 births Category:2017 deaths