- Person
- Martin Karplus
- Lived
- 1930–2024
- Field
- Theoretical chemistry
- From
- Austrian-American
The story
Martin Karplus was born in Vienna in 1930 into a secular Jewish family. A few days after the Nazi takeover of Austria in March 1938 his mother fled with him and his brother to Switzerland, while his father was held in a Vienna jail; the family reached New York that October as refugees. Karplus grew up near Boston, studied at Harvard and Caltech, and became a theoretical chemist who wanted his work to be useful to experimental scientists, not only to other theorists.
Around 1970, after visiting Shneior Lifson’s group at the Weizmann Institute in Israel, he began building computer models of the forces between the atoms of large biological molecules. With his graduate student Bruce Gelin he wrote a program that could take the amino-acid sequence and structure of a protein and calculate the energy and the force on every atom. The next step was to let the atoms move according to Newton’s laws of motion. Chemistry colleagues told him it was impossible; biologists told him it would be a waste of time.
In 1977 his group, with Andrew McCammon, published the first molecular dynamics simulation of a protein, a small molecule called bovine pancreatic trypsin inhibitor. It showed that proteins are not rigid, as crystal structures suggest, but constantly flexing, and that this motion is part of how they work. The program grew into CHARMM, developed by Karplus and his former students and distributed worldwide to universities and companies. Methods that came out of his group’s early simulations became widely used in drug design.
When Karplus shared the 2013 Nobel Prize in Chemistry with Michael Levitt and Arieh Warshel, the Royal Swedish Academy of Sciences said computer models mirroring real life had become crucial for most advances in chemistry, using the example of simulating how a drug couples to its target protein in the body. Today researchers use simulations descended from this work to study how proteins fold and misfold, how enzymes work and how candidate medicines might bind before they are made in a laboratory. Karplus dedicated his Nobel lecture to the 244 students and colleagues who had worked in his laboratories.
Why it matters
Molecular simulations of the kind Karplus pioneered help scientists everywhere understand diseases at the atomic level and design new medicines faster.
About Martin Karplus
Vienna-born refugee who taught computers to show molecules in motion. His CHARMM simulations of proteins are now a standard tool for designing drugs and understanding life. Nobel Prize 2013.
Sources
- Martin Karplus, Biographical NobelPrize.org
- Press release: The Nobel Prize in Chemistry 2013 NobelPrize.org
- Nobel Laureate Martin Karplus ’51 Remembered as Attentive Mentor, ‘Pioneering’ Chemist The Harvard Crimson
Another act of tikkun olam. This is part of tikkun olam, the Jewish idea of repairing the world, and every one of us can add to it.