Max Perutz, a founding father of molecular biology, died yesterday in Cambridge, United Kingdom. He was 87. Perutz and his colleague John Kendrew were the first to pin down the three-dimensional shape of a protein. Their work on the structure of hemoglobin and myoglobin earned them the 1962 Nobel Prize for Chemistry.
Perutz was born in 1914 in Vienna, Austria. He moved to Cambridge in 1936 to study under eminent x-ray crystallographer J. D. Bernal, and kept working, primarily at Cambridge, until last year. He is most famous for his work on hemoglobin, the molecule that shuttles oxygen from the lungs to the rest of the body and gives blood its deep red hue. Perutz labored for more than 20 years to piece together the protein's three-dimensional structure from two-dimensional x-ray pictures, a feat one biographer likened to capturing the structure of Notre Dame Cathedral by taking close-up pictures with a pinhole camera. Perutz himself called it a "forlorn undertaking." The key, he eventually discovered, was to add heavy atoms such as mercury to the protein and compare how different types of atoms slightly shifted the picture.
When the structure was finally unveiled in 1959, it was a gigantic step toward understanding how proteins work, says Tony Wilkinson, a molecular biologist at the University of York. "Everyone knew the formidable capacity of proteins--but there was no sense of the shape, the three dimensions." After determining the structure, Perutz worked for many more years on hemoglobin and discovered how the protein binds and releases oxygen. He submitted his last paper--on the molecular causes of Huntington's disease--for publication on 20 December.
The field of molecular biology that Perutz helped create has grown tremendously: the Protein Data Bank now holds more than 13,000 protein structures, and nowadays new entries "come thick and fast," Wilkinson says. "How we think about these proteins is based on Perutz's work with hemoglobin and myoglobin. It was terrifically important."