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Fred Sanger - Double Nobel Laureate
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Book description

Considered 'the father of genomics', Fred Sanger (1918–2013) paved the way for the modern revolution in our understanding of biology. His pioneering methods for sequencing proteins, RNA and, eventually, DNA earned him two Nobel Prizes. He remains one of only four scientists (and the only British scientist) ever to have achieved that distinction. In this, the first full biography of Fred Sanger to be published, Brownlee traces Sanger's life from his birth in rural Gloucestershire to his retirement in 1983 from the Medical Research Council's Laboratory of Molecular Biology in Cambridge. Along the way, he highlights the remarkable extent of Sanger's scientific achievements and provides a real portrait of the modest man behind them. Including an extensive transcript of a rare interview of Sanger by the author, this biography also considers the wider legacy of Sanger's work, including his impact on the Human Genome Project and beyond.

Reviews

'Fred Sanger’s innovation and achievements enabled us to read the code of life. His breakthroughs transformed science, medicine, industry and society, and continue to open our eyes to a new knowledge and understanding of how life works … This book provides a rare opportunity to see a glimpse of a remarkable man who changed the world.'

David Bentley - Vice-President and chief scientist, Illumina Inc., Cambridge

'Every student of molecular biology would profit greatly by lingering over Sanger’s own descriptions of the several strategies he attempted and the tools he had to invent to arrive at what is referred to today as Sanger DNA Sequencing … Sanger’s success transformed molecular biology in inestimable ways and his methodology is equally foundational in such varied fields as evolutionary biology, plant breeding, paleontology, anthropology, linguistics, forensics and computer science … Fred Sanger was motivated by the challenge of discovery and believed fervently that through art and science, in their broadest senses, it is possible to make a lasting contribution towards the improvement and enrichment of human life.'

Paul Berg - Stanford University, California

'As this wonderfully illuminating biography of Sanger reveals, his contributions were deceptively simple but profoundly far-reaching … Fred Sanger was truly an extraordinary individual whose influence in modern biological and biomedical sciences cannot be overstated.'

Elizabeth Blackburn - University of California, San Francisco

'Fred Sanger was an extraordinary scientist as is evident from this informative biographical essay, celebrating his life and his contributions to science. To be awarded one Nobel Prize is very rare, to be awarded two, as was the case for Fred, has only been accomplished by four individuals in over one hundred years. His was a truly outstanding life … Fred is one of those few individuals of whom it can be said that they changed the world for ever. This essay gives a personal insight into his science and what he achieved. It allows all of us to be a little closer to this gentle, modest man of genius.'

Sir Paul Nurse - President of the Royal Society, London

'Sanger, typical of many successful scientists, is reserved, even shy so we are fortunate that he offered to be interviewed. This book provides a wide-ranging account of his early life and his scientific career … The biography will provide inspiration and encouragement for aspiring inventors, for whom there is still a great need. Above all, it provides lessons for the funders: to find the next Sanger, they must be prepared to give long term support with strings loosely attached.'

Sir Ed Southern - University of Oxford, from the Foreword

'If you type the word 'Sanger' into a search engine, you may find that the Sanger Institute, Hinxton, Cambridge - named after Fred - comes out on top. I think he wouldn't have minded that. He has a living memorial - better than a statue … Sanger taught us to read the information of life, so that we can begin to understand it.'

Sir John Sulston - founding Director of the Wellcome Trust Sanger Institute, Cambridge

'This intimate biography gives readers an unparalleled glimpse into the life of a scientist who transformed biomedical research. This work is filled with scientific details that will delight a biochemist, is accessible to lay readers, and will certainly inspire budding scientists and established academics alike.'

Source: ISCB Newsletter

'Revealing and fascinating.'

Source: Nature

'The biography is well illustrated, very readable … a fascinating insight into the man, told very much, one feels, the way he would have wanted … [It] is a wonderful introduction to the man and his science. Read it and see what you think.'

Hugh Pelham Source: The Biochemist

'This is a great read and one that I would recommend to any student considering a career in the biological sciences - they will find a hero in Sanger and, in doing so, will be inspired.'

Andy Squires Source: The Biologist

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Contents

Appendix: Complete bibliography of Fred Sanger
Sanger, F. Determination of nucleotide sequences in DNA. Biosci. Rep. 24: 237–253 (2004).
Sanger, F. The early days of DNA sequences. Nat. Med. 3: 267–268 (2001).
Sanger, E, Dowding, M, eds., Selected Papers of Frederick Sanger. Singapore: World Scientific (1996).
Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. 1977. Biotechnology 24: 104–108 (1992).
Sanger, F. Sequences, sequences, and sequences. Ann. Rev. Biochem. 57: 1–28 (1988).
Daniels, DL, Sanger, F, Coulson, AR. Features of bacteriophage λ: analysis of the complete nucleotide sequence. Cold Spring Harb. Symp. Quant. Biol. 47: 1009–1024 (1983).
Sanger, F, Coulson, AR, Hong, GF, Hill, DF, Petersen, GB. Nucleotide sequence of bacteriophage λ DNA. J. Mol. Biol. 162: 729–773 (1982).
Anderson, S, de Bruijn, MH, Coulson, AR, Eperon, IC, Sanger, F, Young, IG. Complete sequence of bovine mitochondrial DNA: conserved features of the mammalian mitochondrial genome. J. Mol. Biol. 156: 683–717 (1982).
Anderson, S, Bankier, AT, Barrell, BG, de Bruijn, MHL, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJH, Staden, R, Young, IG. In Slonimski, PP, Borst, P, Attardi, G, eds., Mitochondrial Genes. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 5–43 (1982).
Sanger, F. Determination of nucleotide sequences in DNA. Science 214: 1205–1210 (1981).
Anderson, S, Bankier, AT, Barrell, BG, de Bruijn, MH, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJ, Staden, R, Young, IG. Sequence and organization of the human mitochondrial genome. Nature 290: 457–465 (1981).
Sanger, F. Determination of nucleotide sequences in DNA. Biosci. Rep. 1: 3–18 (1981).
Sanger, F. Nobel Lecture, 1980: Determination of nucleotide sequences in DNA. In Nobel Prizes, Chemistry 1970–1980. Singapore: World Scientific, pp. 431–447 (1993).
Sanger, F, Coulson, AR, Barrell, BG, Smith, AJ, Roe, BA. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143: 161–178 (1980).
Barrell, BG, Anderson, S, Bankier, AT, de Bruijn, MH, Chen, E, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, Schreier, PH, Smith, AJ, Staden, R, Young, IG. Different pattern of codon recognition by mammalian mitochondrial tRNAs. Proc. Natl Acad. Sci. USA 77: 3164–3166 (1980).
Air, GM, Coulson, AR, Fiddes, JC, Friedmann, T, Hutchison, CA, Sanger, F, Slocombe, PM, Smith, AJ. Nucleotide sequence of the F protein coding region of bacteriophage φX174 and the amino acid sequence of its product. J. Mol. Biol. 125: 247–254 (1978).
Sanger, F, Coulson, AR, Friedmann, T, Air, GM, Barrell, BG, Brown, NL, Fiddes, JC, Hutchison, CA, Slocombe, PM, Smith, M. The nucleotide sequence of bacteriophage φX174. J. Mol. Biol. 125: 225–246 (1978).
Sanger, F, Coulson, AR. The use of thin acrylamide gels for DNA sequencing. FEBS Lett. 87: 107–110 (1978).
Sanger, F, Nicklen, S, Coulson, AR. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74: 5463–5467 (1977).
Sanger, F, Air, GM, Barrell, BG, Brown, NL, Coulson, AR, Fiddes, CA, Hutchison, CA, Slocombe, PM, Smith, M. Nucleotide sequence of bacteriophage φX174 DNA. Nature 265: 687–695 (1977).
Smith, M, Brown, NL, Air, GM, Barrell, BG, Coulson, AR, Hutchison, CA, Sanger, F. DNA sequence at the C termini of the overlapping genes A and B in bacteriophage φX174. Nature 265: 702–705 (1977).
Air, GM, Sanger, F, Coulson, AR. Nucleotide and amino acid sequences of gene G of φX174. J. Mol. Biol. 108: 519–533 (1976).
Air, GM, Blackburn, EH, Coulson, AR, Galibert, F, Sanger, F, Sedat, JW, Ziff, EB. Gene F of bacteriophage φX174: correlation of nucleotide sequences from the DNA and amino acid sequences from the gene product. J. Mol. Biol. 107: 445–458 (1976).
Sanger, F. The Croonian Lecture 1975: Nucleotide sequences in DNA. Proc. R. Soc. Lond. B 191: 317–333 (1975).
Air, GM, Blackburn, EH, Sanger, F, Coulson, AR. The nucleotide and amino acid sequence of the N (5′) terminal region of gene G of bacteriophage φX174. J. Mol. Biol. 96: 703–719 (1975).
Sanger, F, Coulson, AR. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94: 441–448 (1975).
Sanger, F, Donelson, JE, Coulson, AR, Kössel, H, Fischer, D. Determination of a nucleotide sequence in bacteriophage f1 DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 90: 315–333 (1974).
Sanger, F, Donelson, JE, Coulson, AR, Kössel, H, Fischer, D. Use of DNA polymerase I primed by a synthetic oligonucleotide to determine a nucleotide sequence in phage f1 DNA. Proc. Natl Acad. Sci. USA 70: 1209–1213 (1973).
Jeppesen, PGN, Barrell, BG, Sanger, F, Coulson, AR. Nucleotide sequences of two fragments from the coat-protein cistron of bacteriophage R17 ribonucleic acid. Biochem. J. 128: 993–1006 (1972).
Sanger, F. The eighth Hopkins Memorial Lecture: Nucleotide sequences in bacteriophage ribonucleic acid. Biochem. J. 124: 833–843 (1971).
Sanger, F, Brownlee, GG. Methods for determining sequences in RNA. Biochem. Soc. Symp. 30: 183–197 (1970).
Jeppesen, PJN, Nichols, JL, Sanger, F, Barrell, BJ. Nucleotide sequences from bacteriophage R17 RNA. Cold Spring Harb. Symp. Quant. Biol. 35: 13–19 (1970).
Brownlee, GG, Sanger, F. Chromatography of 32P-labelled oligonucleotides on thin layers of DEAE-cellulose. Eur. J. Biochem. 11: 395–399 (1969).
Adams, JM, Jeppesen, PG, Sanger, F, Barrell, BG. Nucleotide sequence from the coat protein cistron of R17 bacteriophage RNA. Nature 223: 1009–1014 (1969).
Labrie, F, Sanger, F. 32P-labelling of haemoglobin messenger and other reticulocyte ribonucleic acids with polynucleotide phosphokinase in vitro. Biochem. J. 114: 29P (1969).
Székely, M, Sanger, F. Use of polynucleotide kinase in fingerprinting non-radioactive nucleic acids. J. Mol. Biol. 43: 607–617 (1969).
Adams, JM, Jeppesen, PG, Sanger, F, Barrell, BG. Nucleotide sequences from fragments of R17 bacterophage RNA. Cold Spring Harb. Symp. Quant. Biol. 34: 611–620 (1969).
Barrell, BG, Sanger, F. The sequence of phenylalanine tRNA from E. coli. FEBS Lett. 3: 275–278 (1969).
Fellner, P, Sanger, F. Sequence analysis of specific areas of the 16S and 23S ribosomal RNAs. Nature 219: 236–238 (1968).
Brownlee, GG, Sanger, F, Barrell, BG. The sequence of 5S ribosomal ribonucleic acid. J. Mol. Biol. 34: 379–412 (1968).
Brownlee, GG, Sanger, F, Barrell, BG. Nucleotide sequence of 5S ribosomal RNA from Escherichia coli. Nature 215: 735–736 (1967).
Brownlee, GG, Sanger, F. Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. J. Mol. Biol. 23: 337–353 (1967).
Sanger, F, Brownlee, GG. A two-dimensional fractionation method for radioactive nucleotides. In Grossman, L, Moldave, K, eds., Methods in Enzymology, vol. XII, Part A, New York: Academic Press, pp. 361–363 (1967).
Sanger, F, Brownlee, GG, Barrell, BG. A two-dimensional fractionation procedure for radioactive nucleotides. J. Mol. Biol. 13: 373–398 (1965).
Larner, J, Sanger, F. The amino acid sequence of the phosphorylation site of muscle uridine diphosphoglucose alpha-1,4-glucan α-4-glucosyl transferase. J. Mol. Biol. 11: 491–500 (1965).
Marcker, K, Sanger, F. N-formyl-methionyl-s-RNA. J. Mol. Biol. 8: 835–840 (1964).
Sanger, F, Bretscher, MS, Hocquard, EJ. A study of the products from a polynucleotide-directed cell-free protein synthesizing system. J. Mol. Biol. 8: 38–45 (1964).
Glazer, AN, Sanger, F. The iodination of chymotrypsinogen. Biochem. J. 90: 92–98 (1964).
Glazer, AN, Sanger, F. Effect of fatty acid on the iodination of bovine serum albumin. J. Mol. Biol. 7: 452–453 (1963).
Sanger, F, Thompson, EO. Halogenation of tyrosine during acid hydrolysis. Biochim. Biophys. Acta 71: 468–471 (1963).
Sanger, F, Hocquard, E. Formation of dephospho-ovalbumin as an intermediate in the biosynthesis of ovalbumin. Biochim. Biophys. Acta 62: 606–607 (1962).
Milstein, C, Sanger, F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem. J. 79: 456–469 (1961).
Naughton, MA, Sanger, F. Purification and specificity of pancreatic elastase. Biochem. J. 78: 156–163 (1961).
Naughton, MA, Sanger, F, Hartley, BS, Shaw, DC. The amino acid sequence around the reactive serine residue of some proteolytic enzymes. Biochem. J. 77: 149–163 (1960).
Sanger, F, Shaw, DC. Amino-acid sequence about the reactive serine of a proteolytic enzyme from Bacillus subtilis. Nature 187: 872–873 (1960).
Sanger, F. Chemistry of insulin. Br. Med. Bull. 16: 183–188 (1960).
Milstein, C, Sanger, F. The amino acid sequence around the serine phosphate in phosphoglucomutase. Biochim. Biophys. Acta 42: 173–174 (1960).
Hartley, BS, Naughton, MA, Sanger, F. The amino acid sequence around the reactive serine of elastase. Biochim. Biophys. Acta 34: 243–244 (1959).
Sanger, F. Nobel Lecture, 1958: The chemistry of insulin. In Nobel Lectures, Chemistry 1942–1962. Amsterdam: Elsevier, pp. 134–146 (1964).
Sanger, F. Chemistry of insulin: determination of the structure of insulin opens the way to greater understanding of life processes. Science 129: 1340–1344 (1959).
Williams, J, Sanger, F. The grouping of serine phosphate residues in phosvitin and casein. Biochim. Biophys. Acta 33: 294–296 (1959).
Harris, JI, Naughton, MA, Sanger, F. Species differences in insulin. Arch. Biochem. Biophys. 65: 427–438 (1956).
Brown, H, Sanger, F, Kitai, R. The structure of pig and sheep insulins. Biochem. J. 60: 556–565 (1955).
Ryle, AP, Sanger, F, Smith, LF, Kitai, R. The disulphide bonds of insulin. Biochem. J. 60: 541–556 (1955).
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 60: 535–540 (1955).
Sanger, F, Thompson, EO, Kitai, R. The amide groups of insulin. Biochem. J. 59: 509–518 (1955).
Sanger, F, Smith, LF, Kitai, R. The disulphide bridges of insulin. Biochem. J. 58: vi–vii (1954).
Ryle, AP, Sanger, F. Disulphide interchange reactions. Biochem. J. 58:v–vi (1954).
Sanger, F. A disulphide interchange reaction. Nature 171: 1025–1026 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 53: 366–374 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysates. Biochem. J. 53: 353–366 (1953).
Sanger, F, Thompson, EO. The amino-acid sequence in the glycyl chain of insulin. Biochem. J. 52: iii (1952).
Sanger, F. The arrangement of amino acids in proteins. Adv. Protein Chem. 7: 1–67 (1952).
Sanger, F, Thompson, EO. The inversion of a dipeptide sequence during hydrolysis in dilute acid. Biochim. Biophys. Acta 9: 225–226 (1952).
Sanger, F, Tuppy, H. The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 49: 481–490 (1951).
Sanger, F, Tuppy, H. The amino-acid sequence in the phenylalanyl chain of insulin. 1. The identification of lower peptides from partial hydrolysates. Biochem. J. 49: 463–481 (1951).
Bailey, K, Sanger, F. The chemistry of amino acids and proteins. Ann. Rev. Biochem. 20: 103–130 (1951).
Sanger, F. Some chemical investigations on the structure of insulin. Cold Spring Harb. Symp. Quant. Biol. 14: 153–160 (1950).
Sanger, F. The chemistry of insulin. Annu. Rep. Prog. Chem. 45: 283–292 (1949).
Sanger, F. Application of partition chromatography to the study of protein structure. Biochem. Soc. Symp. 3: 21 (1949).
Sanger, F. Species differences in insulins. Nature 164: 529 (1949).
Sanger, F. The terminal peptides of insulin. Biochem. J. 45: 563–574 (1949).
Sanger, F. Fractionation of oxidized insulin. Biochem. J. 44: 126–128 (1949).
Sanger, F. Some peptides from insulin. Nature 162: 49 (1948).
Porter, RR, Sanger, F. The free amino groups of haemoglobins. Biochem. J. 42: 287–294 (1948).
Tiselius, A, Sanger, F. Adsorption analysis of oxidized insulin. Nature 160: 433 (1947).
Sanger, F. Oxidation of insulin by performic acid. Nature 160: 295 (1947).
Sanger, F. The free amino group of gramicidin S. Biochem. J. 40: 261–262 (1946).
Sanger, F. The free amino groups of insulin. Biochem. J. 39: 507–515 (1945).
Neuberger, A, Sanger, F. The availability of ε-acetyl-d-lysine and ε-methyl-dl-lysine for growth. Biochem. J. 38: 125–129 (1944).
Neuberger, A, Sanger, F. The metabolism of lysine. Biochem. J. 38: 119–125 (1944).
Neuberger, A, Sanger, F. The availability of the acetyl derivatives of lysine for growth. Biochem. J. 37: 515–518 (1943).
Harris, HA, Neuberger, A, Sanger, F. Lysine deficiency in young rats. Biochem. J. 37: 508–513 (1943).
Sanger, F. The metabolism of the amino-acid lysine in the animal body. PhD thesis, Cambridge University (1943).
Neuberger, A, Sanger, F. The nitrogen of the potato. Biochem. J. 36: 662 (1942).
Selected papers by colleagues
Smith, AJ. The use of exonuclease III for preparing single stranded DNA for use as a template in the chain terminator sequencing method. Nucl. Acids Res. 6: 831–848 (1979).
Barrell, BG, Bankier, AT, Drouin, J. A different genetic code in human mitochondria. Nature 282: 189–194 (1979).
Friedmann, T, Brown, DM. Base-specific reactions useful for DNA sequencing: methylene blue-sensitized photooxidation of guanine and osmium tetraoxide modification of thymine. Nucl. Acids Res. 5: 615–622 (1978).
Barrell, BG, Air, GM, Hutchison, CA. Overlapping genes in bacteriophage φX174. Nature 264: 34–41 (1976).
Blackburn, EH. Transcription and sequence analysis of a fragment of bacteriophage φX174 DNA. J. Mol. Biol. 107: 417–431 (1976).
Sedat, J, Ziff, E, Galibert, F. Direct determination of DNA nucleotide sequences: structure of large specific fragments of bacteriophage φX174 DNA. J. Mol. Biol. 107: 391–416 (1976).
Blackburn, EH. Transcription by Escherichia coli RNA polymerase of a single-stranded fragment by bacteriophage φX174 DNA 48 residues in length. J. Mol. Biol. 93: 367–374 (1975).
Galibert, F, Sedat, J, Ziff, E. Direct determination of DNA nucleotide sequences: structure of a fragment of bacteriophage φX174 DNA. J. Mol. Biol. 87: 377–407 (1974).
Ziff, EB, Sedat, JW, Galibert, F. Determination of the nucleotide sequence of a fragment of bacteriophage φX174 DNA. Nat. New Biol. 241: 34–37 (1973).
Ling, V. Pyrimidine sequences from the DNA of bacteriophages fd, f1, and φX174. Proc. Natl Acad. Sci. USA 69: 742–746 (1972).
Ling, V. Fractionation and sequences of the large pyrimidine oligonucleotides from bacteriophage fd DNA. J. Mol. Biol. 64: 87–102 (1972).
Dahlberg, JE. Terminal sequences of bacteriophage RNAs. Nature 220: 548–552 (1968).
Dube, SK, Marcker, KA, Clark, BF, Cory, S. Nucleotide sequence of N-formyl-methionyl-transfer RNA. Nature 218: 232–233 (1968).
Murray, K, Offord, RE. Use of neutron activation in the characterization of small quantities of nucleic acids. Nature 211: 376–378 (1966).

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