- Person
- Max Perutz
- Lived
- 1914–2002
- Field
- Molecular biology
- From
- Austrian-British
The story
Most scientists slow down in their eighties. Max Perutz retired as chairman of the Laboratory of Molecular Biology in Cambridge in 1979, but he kept working in the laboratory almost every day and published more than 100 papers and articles in his retirement. Asked once why he had not retired at 65, he said he had been tied up in some very interesting research at the time. In his final years he took on a new and urgent problem: the protein changes behind Huntington's disease and other neurodegenerative disorders.
Huntington's disease is caused by a gene in which a short DNA sequence, the triplet CAG, is repeated too many times. Each repeat adds one unit of the amino acid glutamine to the protein the gene makes, producing an abnormally long polyglutamine stretch. Several inherited brain disorders, including some spinocerebellar ataxias, arise in the same way, and in general the longer the stretch, the earlier in life the disease tends to appear.
Perutz brought a structural biologist's eye to the problem. He developed a strong interest in the structure of these polyglutamine tracts and proposed that glutamine stretches can bind together into what he called a polar zipper, linking protein chains and causing them to clump. He demonstrated that the age at which Huntington's disease begins is related to the number of glutamine repeats, connecting the molecular structure to the course of the illness.
He kept working until the very end. He was active in the laboratory almost every day until the Friday before Christmas in 2001 and submitted his last paper just a few days before that. He died of cancer in Cambridge on 6 February 2002, at the age of 87.
His late work helped focus attention on protein aggregation. Proteins with long polyglutamine stretches are now known to be increasingly prone to forming clumps that build up into fibrous deposits, sharing features with the amyloid found in other brain diseases. Understanding why these proteins stick together is a key question for scientists studying Huntington's disease.
Why it matters
Perutz's insight into protein clumping contributed to a major line of research into devastating brain diseases.
About Max Perutz
Viennese refugee who spent 22 years solving the structure of haemoglobin, won the 1962 Nobel Prize and built the Cambridge laboratory where molecular biology came of age.
More about Max Perutz
- Max Perutz founded the unit where DNA's shape was foundIn 1947 Max Perutz obtained Medical Research Council support for a small unit to study biological molecules; Watson and Crick built their DNA model there in 1953.
- Max Perutz was also a pioneering glacier scientistIn 1938 Max Perutz joined a three-man expedition to study how snow becomes glacier ice in Switzerland, work that made him an expert on glaciers.
- Perutz explained how haemoglobin delivers oxygenIn 1970 Max Perutz proposed how haemoglobin works as a molecular machine, switching shape to pick up oxygen in the lungs and release it in the tissues.
- Perutz linked haemoglobin's shape to inherited diseaseMax Perutz studied how changes in haemoglobin's amino acids alter its function, hoping to find drugs for genetic blood disorders such as sickle cell anaemia.
- Max Perutz found the key to seeing protein structuresIn 1953 Max Perutz showed that attaching heavy atoms such as mercury to protein crystals solves the X-ray 'phase problem', making protein crystallography possible.
- Perutz led a lab whose scientists shared 12 Nobel PrizesMax Perutz founded and chaired the MRC Laboratory of Molecular Biology in Cambridge from 1962 to 1979; its scientists have shared 12 Nobel Prizes.
- Max Perutz revealed the structure of haemoglobinIn 1959, 22 years after he began, Max Perutz determined the structure of haemoglobin, the blood's oxygen carrier, sharing the 1962 Nobel Prize in Chemistry.
Sources
- Max Perutz Wikipedia
- Max Perutz American Crystallographic Association history
- Max Ferdinand Perutz (obituary by Francis Crick) Physics Today
- Polyglutamine tract Wikipedia
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.