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Sequences, conformation, information: Biochemists and molecular biologists in the 1950s

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References

  1. Among others, see Biochemistry, “Molecular Biology” and the Biological Sciences: Report of a Subcommittee of the Biochemical Society on the Report of the Working Group on Molecular Biology (“Kendrew Report”) and the Present State of Biological Sciences in this Country, with Particular Reference to Biochemistry (London: Biochemical Society, 1969); T. W. Good-win, British Biochemistry Past and Present: Biochemical Society Symposium No. 30, held in London, December 1969 (London and New York: Academic Press, 1970), especially the “Chairman's Introduction” by J. N. Davidson, pp. 3–4; E. Chargaff, “The Tower of Babel,” Nature, 248 (1974), 776–797; S. S. Cohen, “The Origins of Molecular Biology,” Science, 187 (1975), 827–830; idem, “The Biochemical Origins of Molecular Biology: Introduction,” Trends Biochem. Sci., 9 (1984), 334–336; The Origins of Modern Biochemistry: A Retrospect on Proteins, Ann. N. Y. Acad. Sci., 325 (1979); and J. S. Fruton, A Skeptical Biochemist (Cambridge, Mass.: Harvard University Press, 1992), esp. pp. 195–214.

  2. See R. Olby, “Biochemical Origins of Molecular Biology,” Trends Biochem. Sci., 11 (1986), 303–305; N. Morgan and R. Olby, “Practising without a License: Discipline Identity in Biochemistry and Molecular Biology” (unpublished paper); P. G. Abir-Am, “The Politics of Macromolecules: Molecular Biologists, Biochemists, and Rhetoric,” Osiris, 7 (1992), 210–237.

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  3. See the statements of Monod and Brenner in H. F. Judson, The Eighth Day of Creation: Makers of the Revolution in Biology (London: Jonathan Cape, 1979), pp. 213, 231; interview with S. Brenner, Cambridge, July 17, 1992; interview with F. Crick, Cambridge, May 25, 1993. Surprisingly, Cohen, when claiming a place for biochemistry in the history of molecular biology, did not mention protein sequencing among the techniques biochemists had contributed to the development of the field; see Cohen, “Biochemical Origins” (above, n. 1).

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  4. E.g., F. Crick, “On Protein Synthesis,” in The Biological Replication of Macromolecules, Symposia of the Society of Experimental Biology XII (Cambridge: Cambridge University Press, 1958), p. 158.

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  8. F. Sanger, “Sequences, Sequences, and Sequences”, Ann. Rev. Biochem., 57 (1988), 4. Sanger referred to the X-ray crystallographer William Astbury as the chief proponent of stoichiometry and to the theory of Max Bergmann and Carl Niemann as the most popular hypothesis of protein structure in those days. Both “Bill” Pirie and Albert Neuberger, with whom Sanger studied as a Ph.D. student, had questioned the Bergmann-Niemann hypothesis. According to Sanger, a useful outcome of that theory was that it stimulated an interest in amino acid analysis (see ibid.). For earlier work on proteins based on the notion of sequence as a determinant of biological specificity, see R. Olby, “Historical Aspects of Protein Structure” (typescript 1985); idem, The Path to the Double Helix: The Discovery of DNA (New York: Dover, 1994), pp. xxv, 74 ff.

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  9. Sanger was also a conscientious objector and had been given exemption form military service: Sanger, “Sequences” (above, n. 8), p. 2.

  10. Among them were Kenneth Bailey, Ernst Frank Williams, Maurice William Rees, George Roland Tristram, and Hebert Taylor Macpherson.

  11. A. C. Chibnall, “Amino-Acid Analysis and the Structure of Proteins”, Proc. Roy. Soc. London, ser. B, 131 (1942), 155. In the same lecture Chibnall challenged the Bergmann-Niemann hypothesis on the basis of his highly accurate amino acid analysis.

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  12. Chibnall Papers, files B20 and B21, University Archives, University Library, Cambridge, England. Eli Lilly supported Chibnall's research on insulin from 1951 to 1958, with only a short interruption.

  13. S. W. Fox, “Terminal Amino Acids in Peptides and Proteins,” Adv. Protein Chem., 2 (1945), 155–177.

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  14. Chibnall's and Sanger's accounts of these events differ slightly. For Chibnall's version see A. C. Chibnall, Early Days in Biochemistry (London: Biochemical Society, 1987), pp. 31–32. For Sanger's commentary on Chibnall's account see J. S. Fruton, A Skeptical Biochemist (Cambridge, Mass.: Harvard University Press, 1992), p. 36, n. 52.

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  15. See also R. Olby, “The Recasting of the Sciences: The Case of Molecular Biology,” in La ristrutturazione delle scienze tra le due guerre mondiali, ed. G. Battimeli, M. de Maria, and A. Rossi (Rome: La Goliardica, 1986), II, 237–247.

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  17. The history of the development of partition chromatography is recalled by Martin in his Nobel Lecture: A. J. Martin, “The Development of Partition Chromatography,” in Nobel Lectures Including Presentation Speeches and Laureates' Biographies: Chemistry 1942–1962 (Amsterdam, London, and New York: Elsevier, 1964), pp. 359–371. See also R. L. M. Synge, “Applications of Partition Chromatography,” in ibid., pp. 374–387.

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  18. See A. C. Chibnall, Early Days in Biochemistry (London: Biochemical Society, 1987), p. 31.

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  19. F. Sanger, “The Free Amino Groups of Insulin,” Biochem. J., 39 (1945), 507–515. In a later statement on this article, which became a standard reference for the method of endgroup determination, Sanger recalled that the editor of the journal, a distinguished organic chemist, had delayed publication: he required that the new dinitrophenyl-amino acids were characterized, as was customary, by their melting point and elementary analysis, while Sanger had heavily relied on their chromatographic behavior; see F. Sanger, Curr. Contents, 28: 12 (1985), 23. This incident points to the difficulty of introducing new analytical methods into current practices.

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  20. Sanger, Curr. Contents, 28: 12 (1985), 23.

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  21. F. Sanger, “The Terminal Peptides of Insulin,” Biochem. J., 45 (1949), 563–574; idem, “Sequences” (above, n. 8), p. 7.

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  22. Interview with F. Sanger, Cambridge, March 25, 1993. A close reading of Fox's review article of 1945 on end-group determination confirms Sanger's statement. Fox listed the determination of amino acid sequence as one of the purposes of determining terminal amino acids; discussing work pursued in this direction, he argued that the ideal solution would involve “removal of terminal amino acids from a peptide of any length, one at a time, without alteration of the remaining peptide” (Fox, “Terminal Amino Acids” [above, n. 13], p. 157). This approach was pursued by the Swedish biochemist Pehr Edman (see below).

  23. R. Consden, A. H. Gordon, A. J. P. Martin, and R. L. M. Synge, “Gramicidin S: The Sequence of Amino Acid Residues,” Biochem. J., 41 (1947), 596–602. Around the same time that Sanger was developing his sequencing method, Pehr Edman, working at the University of Lund, developed a sequencing method based on the sequential degradation of the polypeptide chain. Edman was not in a favorable position to further his work, and the reception was slow; eventually, however, his method completely superseded Sanger's sequencing method (see below).

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  24. Sanger was first introduced to the technique of radioactive labeling by Chris Anfinsen, who was on sabbatical leave in Sanger's laboratory in 1954. Sanger recalled: “Previously I had assumed that isotopes were in the realm of physicists and that the apparatus and techniques would be beyond my means. But I learned that this was not the case and that already a number of radioactive substrates were available” (Sanger, “Sequences” [above, n. 8], p. 11).

  25. P. Edman, “Method for Determination of the Amino Acid Sequence in Peptides,” Acta Chem. Scan., 4 (1950), 283–293.

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  26. On the development of sequencing techniques by Stein and Moore, see below.

  27. B. S. Hartley, “The Primary Structure of Proteins,” in Goodwin, British Biochemistry Past and Present: Biochemical Society Symposium No. 30, held in London, December 1969 (London and New York: Academic Press, 1970), pp. 29–41. By that time Hartley had moved with Sanger from the Biochemistry Department to the new Laboratory of Molecular Biology in Cambridge. On the disciplinary implication of this move, see below.

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  28. Interview with B. Hartley, Elsworth, September 28, 1992.

  29. In the course of his chemical studies of proteins Hartley also developed new lines of investigation. He chose chymotrypsin, a commercially available pancreatic enzyme, as his research topic, and published the complete sequence of the protein in 1964. By that time his main interest had shifted from enzyme function to evolutionary studies. Comparing the sequences of different pancreatic enzymes, he could show that while chymotrypsin, trypsin, and elastase had a different biological activity, they nevertheless presented a similar sequence. He deduced that they had evolved from a common ancestor, and he proceeded to develop genetic models to account for the evolutionary history of the proteins: B. S. Hartley, “Enzymes are Proteins,” Adv. Sci., 23 (1966), 47–54. A reaction mechanism for chymotrypsin was suggested five years later, on the basis of a three-dimensional model of the molecule that accommodated both X-ray and sequencing data: D. M. Blow, J. J. Birktoft, and B. S. Hartley, “Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin,” Nature, 221 (1969), 337–340. On the interactions between protein chemists and protein crystallographers, see the next section; on the collaboration between Hartley and Blow in their work on chymotrypsin, in particular see also S. de Chadarevian, “Architektur der Proteine: Strukturforschung am Laboratory of Molecular Biology in Cambridge,” in Experimentalsysteme in den biologisch-medizinischen Wissenschaften: Objekte, Differenzen, Konjunkturen, ed. M. Hagner and H.-J. Rheinberger (Berlin: Akademie Verlag, 1994), pp. 181–200.

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  30. At the beginning of the 1950s, Vincent Du Vigneaud and his collaborators, working at Cornell University Medical College, successfully attempted the synthesis of the polypeptide oxytoxin, the uterine-contracting hormone of the pituitary gland, providing proof of the structure they had determined before. It was the first synthesis of a protein-like hormone and gained Du Vigneaud the Nobel Prize in 1955; see V. Du Vigneaud, “A Trail of Sulfur Research: From Insulin to Oxytoxin,” in Nobel Lectures: Chemistry 1942–1962 (Amsterdam, London, and New York: Elsevier, 1964), pp. 446–465.

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  31. Interview with J. Kendrew, Cambridge, July 14, 1993.

  32. On the phase-problem and its solution see D. W. Green, V. Ingram, and M. F. Perutz, “The Structure of Haemoglobin. IV. Sign Determination by the Isomorphous Replacement Method,” Proc. Roy. Soc., ser. A, 225 (1954), 287–329.

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  33. Kendrew had found sperm whale meat for his experiments in the Low Temperature Research Station in Cambridge, where, during the war, the use of whale meat as supplement to butcher's meat was investigated. The meat was black, indicating a high content of myoglobin. Later batches of sperm whale meat were sent to Kendrew by air from Lima, where the meat could be bought on the market; interview with J. Kendrew, London, March 18, 1993.

  34. J. D. Bernal, “X-Ray Evidence for the Structure of Protein Molecules,” in T. Svedberg et al., “A Discussion on the Protein Molecule,” Proc. Roy. Soc. London ser. B, 127 (1939), 38. The meeting at the Royal Society saw the participation of physical chemists, colloidal chemists, biochemists, and X-ray crystallographers. It points to the importance attributed to the topic and exemplifies the intense exchange among practitioners of different disciplinary backgrounds that took place at the time. On the role of protein research in the 1930s, see also L. Kay, The Molecular Vision of Life (Oxford and New York: Oxford University Press, 1993), esp. pp. 104–120.

  35. Interview with J. Kendrew, Linton, March 18, 1993.

  36. Sanger himself was rather critical of Stein and Moore's approach to protein sequencing, which involved complicated apparatuses and a large amount of routine work. He set as his own research agenda the development of simpler and more economical sequencing methods: F. Sanger, “Memorandum to the Medical Research Council” [undated, attached to a letter from Sanger to Mellanby, June 26, 1957], p. 2, file E 242/109, vol. 1, MRC Archive, London.

  37. Kendrew to Moore and Stein, November 2, 1955, Kendrew Papers, file C. 273, Bodleian Library, Oxford.

  38. Ibid.

  39. Ibid.

  40. Ibid.; Lindley, J. S. Rollett, “An Investigation of Insulin Structure by Model Building Techniques,” Biochim. Biophys. Acta, 18 (1955), 183–193. Lindley was on leave from the Wool Textile Research Laboratories in Melbourne, while Rollett was affiliated with the Laboratory of Chemical Crystallography at the University Museum at Oxford, England.

  41. The insight that genes determined the amino acid sequence of proteins was brought home to Kendrew by the work on sickle-cell hemoglobin performed by Vernon Ingram in the same Cambridge laboratory. For more details on Ingram's investigations, see below.

  42. J. C. Kendrew, “Myoglobin and the Structure of Proteins,” in Nobel Lectures Including Presentation Speeches and Laureates' Biographies: Chemistry 1942–1962 (Amsterdam, London, and New York: Elsevier, 1964), p. 696.

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  43. Kendrew to Moore and Stein, November 2, 1955, Kendrew Papers, file C.273, Bodleian Library, Oxford.

  44. Moore to Kendrew, November 29, 1955, ibid.

  45. Kendrew to Moore, December 21, 1955, ibid.

  46. Moore to Kendrew, March 20, 1956, ibid.

  47. In 1962, when the Unit moved from the Cavendish to the new Laboratory of Molecular Biology, Edmundson, even if linked to the X-ray crystallography group, was expected to be located in the division of protein chemistry—that is, with Sanger's group, who had joined the laboratory. Yet the division did not agree to give up space for Edmundson and his amino acid analyzer, which had been shipped over to him from America. He finally ended up in the division of molecular genetics, where some researchers had started to use sequencing techniques (see below). This episode, banal in many respects, still points to the problems of bridging different research cultures, even in innovative institutions like the Laboratory of Molecular Biology, which was designed to encourage collaboration.

  48. J. Kendrew et al., “A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis,” Nature, 181 (1958), 662–666.

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  49. J. Kendrew et al., “A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis,” Nature, 181 (1958), p. 665.

  50. Dr. Norton, “Visit to the Molecular Biology Research Unit, Cambridge, 2nd December 1957,” unpublished internal report, file E 243/29, MRC Archive, London.

  51. See M. W. Wilkes, Memoirs of a Computer Pioneer (Cambridge, Mass.: MIT Press, 1985), p. 192. On the work involved in the 2 Å analysis of myoglobin, see R. E. Dickerson, “A Little Ancient History,” Protein Sci., 1 (1992), 182–186.

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  52. J. Kendrew et al., “A Partial Determination by X-Ray Methods, and Its Correlation by Chemical Data,” Nature, 190 (1961), 666–672.

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  53. A. B. Edmundson and C. H. W. Hirs, “The Amino-Acid Sequence of Sperm Whale Myoglobin,” Nature, 190, (1961), 663–665.

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  54. See H. F. Judson, The Eighth Day of Creation: Makers of the Revolution in Biology (London: Jonathan Cape, 1979), p. 229.

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  55. F. Crick, “On Protein Synthesis” in The Biological Replication of Macromolecules, Symposia of the Society of Experimental Biology XII (Cambridge: Cambridge University Press, 1958), p. 152. Phrased this way, the sequence hypothesis could not have been formulated before the elucidation of the structure of DNA in 1953. Yet Crick maintains that Sanger's first sequencing results suggested to him that the genes would determine the amino acid sequence even before 1953: F. Crick, WhatMad Pursuit: A Personal View of Scientific Discovery (London: Penguin, 1990), p. 36; interview with Crick, Cambridge, May 25, 1993.

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  56. S. Brenner, “On the Impossibility of All Overlapping Triplet Codes in Information Transfer form Nucleic Acids to Proteins”, Proc. Nat. Acad. Sci., 43 (1957), 687.

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  57. F. Crick, “On Protein Synthesis”, in The Biological Replication of Macromolecules, Symposia of the Society of Experimental Biology XII (Cambridge: Cambridge University Press, 1958), p. 144. Note that this was a very strong position to take for someone like Crick, whose main experimental training was in X-ray crystallography.

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  58. F. Crick, “On Protein Synthesis”, in The Biological Replication of Macromolecules, Symposia of the Society of Experimental Biology XII (Cambridge: Cambridge University Press, 1958), p. 153.

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  59. Ibid.

  60. Judson maintained (Wrongly, I think) that “what Chargaff and Sanger did was to reduce the chemistry of [nucleic acids and proteins] to total dependence on information” (Judson, Eighth Day of Creation: Makers of the Revolution in Biology (London: Jonathan Cape, 1979), p. 243). As shown above, for Sanger, in his work on insulin, sequence meant structure, not information.

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  61. F. Crick, “On Protein Synthesis”, in The Biological Replication of Macromolecules, Symposia of the Society of Experimental Biology XII (Cambridge: Cambridge University Press, 1958), p. 158.

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  62. I refer to molecular genetics and not molecular biology in this context,since in Cambridge molecular genetics represented only one division of the larger enterprise of molecular biology that grew out of the alliance of protein crystallographers, molecular geneticists, and protien chemists. In fact, Crick's combative position toward the biochemists did not prevent him and his colleagues in Cambridge from trying to persuade Sanger to join their plans for a new laboratory of molecular biology (see below). Significantly, for Kendrew, molecular biologists distinguished themselves form biochemists by their interest in both information and conformation: see J. C. Kendrew, “Information and Conformation in Biology”, in Structural Chemistry and Molecular Biology: A volume Dedicated to Linus Pauling by His Students, Colleagues and Friends ed. A. Rich and N. Davidson, (San Francisco and London: Freeman, 1968), pp. 187–197.

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  63. J. D. Watson and F. H. C. Crick, “Genetical Implications of the Structure of Deoxyribonucleic Acid,” Nature, 171 (1953), 965.

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  64. F. Crick, “What mad pursuit: A Personal View of Scientific Discovery (London: Penuin, 1990), p. 90; interview with Crick, Cambridge, May 25, 1993. Crick suggested that it would have been more correct to speak of genetic cipher instead of genetic code, since the Morse code was also a cipher, but he did not know that at the time - and besides, it would not have sounded as good. Brenner pointed out that he quickly realized that they wer etalking about messages rather than information, hence also the coinage of the term “messenger RNA” later on (interview with S. Brenner, Cambridge, July 17 1992). The image of the Morse code was also used by Erwin Schrödinger to illustrate the way genes acted in development: E. Schrödinger, What Is Life? The Physical Aspect of the Living Cell with Mind and Matter & Autobiographical Sketches (Cambridge: Cambridge University Press, 1992), p. 61. Fox historical perspectives on the use of the term “information” in the life sciences, see E. Fox-Keller, “The Body of a New Machine: Situating the Organism between Telegraphs and Computers”, in Refiguring Life: Metaphors of Twentieth-Century Biology (New York: Columbia University Press, 1995), pp. 79–118; L. Kay, “Who Wrote the Book of Life? Information and Transformation of Molecular Biology, 1945–1955”, Sci. Context, 8 (1995), 609–634; and idem, Who Wrote the Book of Life? A History of the Genetic Code (Chicago: Chicago University Press, forthcoming), chaps. 1 and 2.

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  65. See F. Crick, “What mad pursuit: A Personal View of Scientific Discovery (London: Penuin, 1990), pp. 103–105

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  66. V. M. Ingram, “A Specific Chemical Difference between the Globins of Normal Human and Sickle-Cell Anaemia Haemoglobin”, Nature, 178 (1956), 792–794; idem, “Gene Mutations in Human Haemoglobin: The Chemical Difference between Normal Human and Sickle-Cell Haemoglobin”, Nature, 180 (1957), 326–328. On the Laboratory careerr of sickle-cell hemoglobin see S. de Chadarevian, “Following Molecules. Hemoglobin between the Clinic and the Laboratory,”, in Molecularising Biology and Medicine. New Practices and Alliances, 1930s–1970s, eds. S. de Chadarevian and H. Kamminga (London: Harwood Academic Publishers, forthcoming).

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  67. F. Crick, “What mad pursuit: A Personal View of Scientific Discovery (London: Penuin, 1990), pp. 106

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  68. See H. F. Judson, The Eighth Day of Creation: Makers of the Revolution in Biology (London: Jonathan Cape, 1979), p. 332. For later experiments that followed the same aim, see S. Brenner and L. Barnett, “Genetic and Chemical Studies on the Head Protein of Bacteriophages T2 and T4”, in Brookhaven Symposia in Biology, vol. 12, Structure and Function of Genetic Elements (Upton, N.Y.: Brookhaven National Laboratory, 1959), pp. 86–94.

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  69. Interview with S. Brenner, Cambridge, June 30, 1993. The first contacts between Crick and Sanger date back to the early 1950s, when James Watson was in Cambridge. The main channel of communication with Sanger was then through Herbert Gutfreund from the Department of Colloid Science, who was estimating the molecular weight of insulin by measuring osmotic pressure, and with whom Crick and Watson were friendly. According to Crick's recollections, they also approached Sanger informally with the suggestion that he move from the Biochemistry Department to the Cavendish; Sanger, however, decided against this, as he did not think he would feel at home in a physics department. The Cavendish group then recruited Vernon Ingram instead: F. Crick, letter to author, January 30, 1906. For Sanger's later decision to negotiate together with the Cavendish group for a common new laboratory, see below.

  70. F. Crick to S. Brenner, October 26, 1956, cited in H.F. Judson, Eight Day of Creatin: Makers of the Revolution in Biology, (London: Jonathan Cape, 1979), p. 331.

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  71. Interview with S. Brenner, Cambridge, June 30, 1993. According to both Brenner and Crick, they also tried to interact with Ernest Gale, who was working on protein biosynthesis in bacteria in the same department as Sanger; yet Gale, apparently, showed no interest, and the attempts failed (interviews with Brenner, Cambridge, June 30, 1993; and with Crick, Cambridge, May 25, 1993). On Gale, see H.-J. Rheinberger, “Comparing Experimental Systems,” J. Hist. Biol., this issue.

  72. F. Crick, “What mad pursuit: A Personal View of Scientific Discovery (London: Penuin, 1990), p. 106. As mentioned before, according to Crick, biochemists became interested in genetics following Ingram's work on the effect of mutations on the amino acid composition of hemoglobin.

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  73. For a reminiscence of that year in Cambridge see M. Hoagland, Toward the Habit of Truth: A Life in Science, (New York and London: Norton, 1990), pp. 97–116.

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  74. Interview with Sanger, Cambridge, March 25, 1993.

  75. Interview with Sanger, Cambridge, May 6, 1993.

  76. A. S. Sarabhai, A. O. W. Stretton, and S. Brenner, “Colinearity of the Gene with the Polypeptide Chain,” Nature201 (1964), 13–17. Evidence for the sequence hypothesis had also come just before from Charles Yanofsky and his collaborators, who were working on mutants of the tryptophane synthetase of E. coli: C. Yanofsky et al. “On the Colinearity of Gene Structure and Protein Structure”, Proc. Nat. Acad. Sci., Washington, 51 (1964), 266–272.

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  77. Interview with Crick, Cambridge, May 25, 1993.

  78. Although the term “molecular biology” had been circulating since the late 1930s, the MRC-Unit for Molecular Biology in Cambridge was, to my knowledge, the first institution to adopt the name in 1957. I will be dealing in more detail with the history of the Laboratory of Molecular Biology in Cambridge in a forthcoming book on the making of molecular biology in postwar Britain.

  79. ”Report to the General Board of their Committee on the Future of the MRC Unit of Molecular Biology and Associated Matters”, General Board Paper 4992, University Archives, University Library, Cambridge.

  80. The same is not true for younger members of his group, who, after some years, did engage in collaborative enterprises with X-ray crystallographers.

  81. Sanger, “Sequences” (above, n. 8), p. 14; “Frederick Sanger” (Autobiography), in Les Prix Nobel. Nobel Prizes. Presentations, Biographies, and Lectures (Stockholm, 1981), p. 142.

  82. Interviews with F. Sanger, Cambridge, March 25, 1992, and October 10, 1994.

  83. Council for Scientific Policy, Report of the Working Group on Molecular Biology (London: Her Majesty's Stationary Office, 1968) (Cmnd. 3675); Biochemistry, “Molecular Biology” and the Biological Sciences (above, n. 1). On the history of the two reports see Morgan and Olby, “Practising without a License,” and Abir-Am, “Politics of Macromolecules” (both in n. 2, above); Abir-Am's paper includes a brief analysis of the differences in the response of British and American biochemists to the rise of molecular biology (pp. 225–226).

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De Chadarevian, S. Sequences, conformation, information: Biochemists and molecular biologists in the 1950s. J Hist Biol 29, 361–386 (1996). https://doi.org/10.1007/BF00127380

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