Max Perutz – Scientist of the Day
Max Perutz, an Austrian/British molecular biologist, was born May 19, 1914, in Vienna.
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Max Perutz – Scientist of the Day
Max Perutz, an Austrian/British molecular biologist, was born May 19, 1914, in Vienna.
Learn more...
Max Perutz was born on May 19, 1914. An Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of hemoglobin and myoglobin. At Cambridge he founded and chaired (1962–79) The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB), fourteen of whose scientists have won Nobel Prizes. Perutz’s contributions to molecular biology in Cambridge are documented in The History of the University of Cambridge: Volume 4 (1870 to 1990) published by the Cambridge University Press in 1992.
Max Ferdinand Perutz was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the...
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Perutz's interest piqued Ingram's.
"In the Name of Eugenics: Genetics and the Uses of Human Heredity" - Daniel J. Kevles
Max Perutz & John Kendrew, NOBEL PRIZE LECTURES, 11 December 1962.
Allan Cormack’ & Godfrey Hounsfield’, “Computed Tomography”, NOBEL PRIZE LECTURES, 8 December 1978 was the topic of an earlier blog post. Here I present: Max Perutz, “X-ray Analysis of Heamaglobin”; and, John Kendrew, “Myoglobin and the Structure of Proteins”, NOBEL PRIZE LECTURES, 11 December 1962. Hemoglobin is a protein normally in the blood at concentrations of 12-20 grams per deciliter. The…
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Sir John Cowdery Kendrew (1917-1997), British biochemist, crystallographer and Nobel laureate, with a model of the structure of myoglobin. Kendrew graduated from the University of Cambridge in 1939. After the war, he and Max Perutz studied the crystalline structure of the muscle protein myoglobin using X-ray diffraction techniques. Kendrew, elected a Fellow at Peterhouse College, adapted Perutz's method and by 1959 had identified the structure of myoglobin. Kendrew and Perutz shared the 1962 Nobel Prize in Physiology or Medicine for their work. Kendrew was knighted in 1974.
Max Perutz - Scientist of the Day
Max Perutz, an Austrian-English molecular biologist, was born May 19, 1914, in Vienna. At the Cavendish Labs at Cambridge, he began the pursuit of the molecular structure of hemoglobin. The only tool at hand for probing the structure of a molecule was X-ray crystallography, which had been developed by the father-and-son team of William and Lawrence Bragg at the Cavendish in 1912. In hindsight, trying to come up with a three-dimensional picture of hemoglobin was an absurd challenge; the Braggs had worked on such problems as the crystalline structure of sodium chloride, which has 2 atoms and a molecular weight of 58. Hemoglobin, it would turn out, contains 1000 atoms, has a molecular weight of around 65,000, and consists of four separate chains of proteins bound to what are called heme groups, where the iron atoms are found (and where the oxygen gets bound). But hemoglobin can be crystallized (a necessity when using X-ray crystallography), and it is thoughtfully colored red, which means the crystals are visible and can be sorted by hand under the microscope. Perutz worked on the problem for decades, interrupted by the War, and made his big breakthrough in 1953, when he discovered that adding heavy atoms like mercury to the hemoglobin would change the structure and alter the X-ray interference patterns in meaningful ways, allowing the three-dimensional structure to be gradually inferred. Perutz had what he called a low-resolution model ready by 1959, and this was enough for the Nobel committee, which awarded him the Nobel Prize for Chemistry in 1962 (which he shared with his student John Kendrew). The Nobel committee cleverly arranged that the Prize in Physiology for that same year would go to James Watson and Francis Crick, for their discovery of the structure of DNA. Both achievements came out of the Cavendish Lab in that annus mirabilis of 1953. Perutz finally completed his high-resolution model of hemoglobin in 1970, and was able to show not only what hemoglobin looks like, but how it works. The model is quite something to behold. The little white square in the right foreground contains a model of sodium chloride, whose structure the Braggs had worked so hard to determine in 1912.
Dr. William B. Ashworth, Jr., Consultant for the History of Science, Linda Hall Library and Associate Professor, Department of History, University of Missouri-Kansas City
A discovery is like falling in love and reaching the top of a mountain after a hard climb all in one, an ecstasy induced not by drugs but by the revelation of a face of nature that no one has seen before.
Max Perutz