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Max Perutz's Achievements: How Did He Do Protein Science (1994), 3:1625-1628. Cambridge University Press. Printed in the USA. Copyright 0 1994 The Protein Society ”. ” ” ~~ ”” . .. .. INVITED TRIBUTE, SPECIAL SECTION IN HONOR OF MAX PERUTZ Max Perutz’s achievements: How did he do it? DAVID EISENBERG UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, Molecular Biology Institute, and Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, California 90024-1570 This issue of Protein Science honors the 80th birthday of Max sin, which Bernal and Dorothy Crowfoot Hodgkin had obtained Perutz, oneof the great contributorsto our science. Other great the year before. Professor Mark claimed he was so excited by contributors include EmilFischer, who showed that proteins are these photos that he forgot aboutPerutz’s request to workwith polymerized peptides; James Sumner, who proved decisively Hopkins and instead arranged for him to work with Bernal. that enzymes are proteinsby crystallizing urease; Fred Sanger, When Perutz heard about this, he protested that he knew no who determined the amino acid sequence of insulin, and later crystallography. Professor Mark replied: “Never mind, my boy, along with Gilbert gave us accurate and rapidways to determine you will learn it.” DNA sequences fromwhich protein sequences can be derived; And so Perutz joined Bernal’s lab in September 1936. Perutz and Linus Pauling, who came with up the basic secondary struc- (1980) recalls Bernal as “the mostbrilliant talker I have ever en- tures, the a-helix and 0-sheets. These were all great discover- countered . [and] was soon inspired by [Bernal’s] visionary ies. But Max Perutz gave us the method for determining the faith in the power of X-ray diffraction to solve the structures 3-dimensional structures of proteins and also provided the in- of molecules as large and complex as enzymes or viruses at a tellectual environment thatled to thediscovery of the structure time when the structure of ordinary sugar was still unsolved” of DNA. He hasbeen perhaps the greatest leaderin the merger (Perutz, 1985a). of chemistry with biology and is regarded by all as one of the But Ph.D. dissertations are not based on inspiration alone. principal protein scientists of the century. By the following summer, Perutz still had no thesis topic and was concerned about his future (Perutz,1980). When he returned to Austria for summer vacation, he remembered that onehis of The path to protein structure cousins in Prague had married a biochemist, Felix Haurowitz, How did Perutz comedevelop to a method to reveal the 3-dimen- and Perutzcalled on him for advice. Haurowitzsuggested as a sional structures ofproteins? It was through a series of accidents thesis the structure of hemoglobin. Apparently, like Perutz, he and then single-minded persistence.’ His father was an Austrian did notrealize that itwas then impossible to determine protein textile manufacturer who had spent his apprenticeship in En- structures: there was as yet no practical way to measure accu- gland (Perutz, 1980). As an ardent Anglophile, the father was rately so many intensities of diffraction; therewas no way to de- willing to underwrite the son’s graduate educationin Cambridge, termine the unknown phases of the diffracted beams; and there England. Max Perutz, as an undergraduate at theUniversity of were no computers, or even calculators, to compute electron Vienna in 1935, had learned of the work in Cambridge by Fred- density maps. Haurowitz showed that as oxygen enters hex- erick Gowland Hopkins on vitamins. When he heard that his agonal plates of horse deoxyhemoglobin, they disorder and physical chemistry professor from Vienna, Herman Mark,was monoclinic needles of oxyhemoglobin form in their place going to attenda meeting in Cambridge, Perutz asked Mark to (Haurowitz, 1938). This must mean thatoxygen changes hemo- find a place for him in Hopkins’s laboratory. However, while globin’s shape, and Perutz wanted tosee how. He got down to in Cambridge, Professor Markvisited J.D. Bernal, whoshowed work, not knowing that it would take him 22 years, even to make him the first good X-ray diffraction pictures a of protein, pep- a start. At first Perutz tried to determine the phasesby scanning the ~ ~~~_______________.___.~ Reprint requests to: David Eisenberg, UCLA-DOE Laboratory of molecular transform,using the diffraction pattern of hemoglo- Structural Biology and Molecular Medicine, MolecularBiology Insti- bin crystals in different stages of swelling and shrinkage. Here- tute, and Departmentof Chemistry and Biochemistry, University of Gal- calls (Perutz, 1985a): “. with immense labor I mapped out the ifornia at LOSAngeles, Los Angeles, California 90024-1570; e-mail: nodes and antinodes of the molecular transform of hemoglo- [email protected]. bin, . but managed to determine thesigns of only a few low- ’ Fortunately, Max Perutz has written about his development as a order hol reflections. I also spent many years collecting and scientist and of his process of discovery. In this editorial, I have drawn from these sources, and 1 have freely quoted and paraphrased from visually measuring the intensities of the reflections needed for them. The most extensive sourceis Perutz’s 1989 book, Is Science Nee- a three-dimensional Patterson at 2.8 A resolution, hoping that essary?, which is recommended with enthusiasm to all protein scientists. some simplifying regular features of the molecular structure 1625 1626 D. Eisen berg would make that Patterson interpretable.I did in fact fool my- Success at last self into believing that I had solved the structure of hemoglo- bin, only to find my solution demolished by my newly arrived Nevertheless, from 1953 onward, there was steady progress: research student Francis Crick. I was desperate that 16 years’ a projection map of hemoglobin in 1954 (Bragg & Perutz, 1954); toil had led me nowhere. .” a second heavy-atom derivative finally in 1958; a method by But just then, in 1953, renewed hope arrived in the form of Michael Rossmann (1960) (The Protein Society’s 1994 Stein and a reprint, from Austin Riggs at Harvard, showing that it was Moore Awardee) for determining the relative positions in the possible to bind mercury to hemoglobin. When Perutz exam- unit cell of the 2 heavy atoms; and at last,in 1960, a paper by ined X-ray pictures of hemoglobin with bound mercury, hesaw Perutz, Rossmann and othersdescribing the tertiary and quater- that therewere marked changes in the relative intensities of the nary structureof hemoglobin at 5.5 A resolution (Perutz et al., diffraction spots. He said that this,“. was the most exciting 1960). Meanwhile, Perutz’s colleague and former student, John moment in all my research career, because I realized at that mo- Kendrew, had pressed ahead to apply isomorphous replacement ment that now in principle, the protein problem was solved” to the smaller myoglobin molecule. With myoglobin, but not at (Judson, 1979). In September 1953, he reported this finding at first with hemoglobin, heavy atoms could be bound between the Pasadena Conference on the Structure of Proteins, orga- molecules in the crystal lattice, and,by 1960, it was possible to nized by Linus Pauling. But the conferees took little notice of build an atomic model of the structure at2 A resolution (Ken- his talk. The attention instead went to Linus Pauling and his drew et al., 1960). “Today this lookslike child’s play,” recalled a-helix and to Watson and Crick for theirnew DNA structure. Perutz (1985a) about the 6-A-resolution myoglobin structure of This structure hadbeen worked out in Perutz’s lab, where Wat- 1959, “but remember that the phase angles had to be determined son had come as a postdoc to apply X-ray diffraction to the manually by superposition of circles for each reflection. study of DNA, and where Crick was a graduate student. Nearly all the methods used had to be developed from scratch Even though the method of addingheavy atoms to proteins as the work progressed.” was the solutionin principle to the problem of protein structure, The photograph of the 1962 Nobel Prize ceremony (Fig. I) Perutz found in practice that, “There were all kinds of dread- shows a beaming Perutz, who, alongwith Kendrew, received the ful complications. In retrospect, 6 years doesn’t seem such a ter- award in chemistry. Fortunately, neither awards norscientific ribly long time, but when you’re actually living six years, and fame quenched Perutz’s curiosity about hemoglobin. He and his trying, not very successfully, to apply this method which you coworkers extended the resolution of the hemoglobin structure knew could solve the structureof proteins, it seemed an eternity” to 2.8 A (Perutz et al., 1968) and then to 1.74 A (Fermi et al., (Judson, 1979). 1984). Perutz (1970) presented a detailed atomic model for the Fig. 1. In 1962, Perutz (second from left) and Kendrew(on right) received the Nobel Prize in chemistry. At the same ceremony, \Watson (second from risht) and Crick (third from left)received the award in physiology and medicine, sharing it with Maurice Wilkins from London (on left). The fourth principal in the DNA structure, Rosalind Franklin, had died at age 37, 4 years before. At the center is John Steinbeck, the literature awardee. (Photograph made available by UPI/Bettmann.) Max Perutz and protein science 1627 stereochemical basis of cooperative binding of oxygen, and he tein Society members know enough about the propertiesice of and coworkers explained the effects on hemoglobinphysiology to understand what this means for the volumeice of below the pH and of dozens of mutants species and differences. Onecol- water), and with a cruising range of 7,000 miles. Its displace- league recently heard Perutz speak on an unexpected mutation ment of 2.2 million tons was 26 times that of the QueenEliza- in high-altitude globins.
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