Frederick Sanger

Frederick Sanger is an English Biochemist and two time Nobel Laureate in Chemistry. He was awarded the Nobel Prize in Chemistry 1958 for his work on the structure of proteins (especially insulin) and in 1980 he shared the Nobel Prize in Chemistry with Walter Gilbert and Paul Berg. Gilbert and Sanger shared half of the prize for their breakthrough in the determination of nucleic acid base sequence.

Frederick Sanger proved that proteins have a defined chemical composition. He successfully determined the complete amino acid sequence of two polypeptide chains of Bovine Insulin. Sanger developed “dideoxy “chain termination method for sequencing DNA molecule. This method was used to sequence human mitochondrial DNA, bacteriophage DNA and eventually entire human genome.

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Chemist CHEMIST (structure of proteins, especially that of insulin)
MC 85037634 8
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1958 Nobel Prize in Chemistry for ”work on the structure of proteins, especially that of insulin”

1980 Nobel Prize in Chemistry for ”contributions concerning the determination of base sequences in nucleic acids”

1951 Corday–Morgan Medal

1969 Royal Medal

1971 Gairdner Foundation International Award

1977 Copley Medal

1978 G.W. Wheland Award

1979 Louisa Gross Horwitz Prize

1979 Albert Lasker Award for Basic Medical Research

1994 Association of Biomolecular Resource Facilities Award

1. Sanger Frederick. Determination of nucleotide sequences in DNA. Bioscience reports 2004;24(4-5):237-53.

2. Sanger F. The early days of DNA sequences. Nature medicine 2001;7(3):267-8.

3. Sanger F; Nicklen S; Coulson A R. DNA sequencing with chain-terminating inhibitors. 1977. Biotechnology (Reading, Mass.) 1992;24():104-8.

4. Sanger F. Sequences, sequences, and sequences. Annual review of biochemistry 1988;57():1-28.

5. Daniels D L; Sanger F; Coulson A R. Features of bacteriophage lambda: analysis of the complete nucleotide sequence. Cold Spring Harbor symposia on quantitative biology 1983;47 Pt 2():1009-24.

6. Sanger F; Coulson A R; Hong G F; Hill D F; Petersen G B. Nucleotide sequence of bacteriophage lambda DNA. Journal of molecular biology 1982;162(4):729-73.

7. Anderson S; de Bruijn M H; Coulson A R; Eperon I C; Sanger F; Young I G. Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome. Journal of molecular biology 1982;156(4):683-717.

8. Sanger F. Determination of nucleotide sequences in DNA. Science (New York, N.Y.) 1981;214(4526):1205-10.

9. Anderson S; Bankier A T; Barrell B G; de Bruijn M H; Coulson A R; Drouin J; Eperon I C; Nierlich D P; Roe B A; Sanger F; Schreier P H; Smith A J; Staden R; Young I G. Sequence and organization of the human mitochondrial genome. Nature 1981;290(5806):457-65.

10. Sanger F. Determination of nucleotide sequences in DNA. Bioscience reports 1981;1(1):3-18.

11. Sanger F; Coulson A R; Barrell B G; Smith A J; Roe B A. Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. Journal of molecular biology 1980;143(2):161-78.

12. Barrell B G; Anderson S; Bankier A T; de Bruijn M H; Chen E; Coulson A R; Drouin J; Eperon I C; Nierlich D P; Roe B A; Sanger F; Schreier P H; Smith A J; Staden R; Young I G. Different pattern of codon recognition by mammalian mitochondrial tRNAs. Proceedings of the National Academy of Sciences of the United States of America 1980;77(6):3164-6.

13. Air G M; Coulson A R; Fiddes J C; Friedmann T; Hutchison C A; Sanger F; Slocombe P M; Smith A J. Nucleotide sequence of the F protein coding region of bacteriophage phiX174 and the amino acid sequence of its product. Journal of molecular biology 1978;125(2):247-54.

14. Sanger F; Coulson A R; Friedmann T; Air G M; Barrell B G; Brown N L; Fiddes J C; Hutchison C A; Slocombe P M; Smith M. The nucleotide sequence of bacteriophage phiX174. Journal of molecular biology 1978;125(2):225-46.

15. Sanger F; Coulson A R. The use of thin acrylamide gels for DNA sequencing. FEBS letters 1978;87(1):107-10.

16. Sanger F; Nicklen S; Coulson A R. DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences of the United States of America 1977;74(12):5463-7.

17. Sanger F; Air G M; Barrell B G; Brown N L; Coulson A R; Fiddes C A; Hutchison C A; Slocombe P M; Smith M. Nucleotide sequence of bacteriophage phi X174 DNA. Nature 1977;265(5596):687-95.

18. Smith M; Brown N L; Air G M; Barrell B G; Coulson A R; Hutchison C A; Sanger F. DNA sequence at the C termini of the overlapping genes A and B in bacteriophage phi X174. Nature 1977;265(5596):702-5.

19. Air G M; Sanger F; Coulson A R. Nucleotide and amino acid sequences of gene G of omegaX174. Journal of molecular biology 1976;108(3):519-33.

20. Air G M; Blackburn E H; Coulson A R; Galibert F; Sanger F; Sedat J W; Ziff E B. Gene F of bacteriophage phiX174. Correlation of nucleotide sequences from the DNA and amino acid sequences from the gene product. Journal of molecular biology 1976;107(4):445-58.

21. Sanger F. The Croonian Lecture, 1975. Nucleotide sequences in DNA. Proceedings of the Royal Society of London. Series B, Containing papers of a Biological character. Royal Society (Great Britain) 1975;191(1104):317-33.

22. Air G M; Blackburn E H; Sanger F; Coulson A R. The nucleotide and amino acid sequences of the N (5’) terminal region of gene G of bacteriophage phiphiX 174. Journal of molecular biology 1975;96(4):703-19.

23. Sanger F; Coulson A R. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. Journal of molecular biology 1975;94(3):441-8.

24. Sanger F; Donelson J E; Coulson A R; Kössel H; Fischer D. Determination of a nucleotide sequence in bacteriophage f1 DNA by primed synthesis with DNA polymerase. Journal of molecular biology 1974;90(2):315-33.

25. Sanger F; Donelson J E; Coulson A R; Kössel H; Fischer D. Use of DNA polymerase I primed by a synthetic oligonucleotide to determine a nucleotide sequence in phage fl DNA. Proceedings of the National Academy of Sciences of the United States of America 1973;70(4):1209-13.

26. Jeppesen P G; Barrell B G; Sanger F; Coulson A R. Nucleotide sequences of two fragments from the coat-protein cistron of bacteriophage R17 ribonucleic acid. The Biochemical journal 1972;128(5):993-1006.

27. Sanger F. Nucleotide sequences in bacteriophage ribonucleic acid. The eighth hopkins memorial lecture. The Biochemical journal 1971;124(5):833-43.

28. Sanger F; Brownlee G G. Methods for determining sequences in RNA. Biochemical Society symposium 1970;30():183-97.

29. Brownlee G G; Sanger F. Chromatography of 32P-labelled oligonucleotides on thin layers of DEAE-cellulose. European journal of biochemistry / FEBS 1969;11(2):395-9.

30. Adams J M; Jeppesen P G; Sanger F; Barrell B G. Nucleotide sequence from the coat protein cistron of R17 bacteriophage RNA. Nature 1969;223(5210):1009-14.

31. Labrie F; Sanger F. 32P-labellingof haemoglobin messenger and other reticulocyte ribonucleic acids with polynucleotide phosphokinase in iro. The Biochemical journal 1969;114(2):29P.

32. Adams J M; Jeppesen P G; Sanger F; Barrell B G. Nucleotide sequences from fragments of R17 bacterophage RNA. Cold Spring Harbor symposia on quantitative biology 1969;34():611-20.

33. Fellner P; Sanger F. Sequence analysis of specific areas of the 16S and 23S ribosomal RNAs. Nature 1968;219(5151):236-8.

34. Brownlee G G; Sanger F; Barrell B G. The sequence of 5 s ribosomal ribonucleic acid. Journal of molecular biology 1968;34(3):379-412.

35. Brownlee G G; Sanger F; Barrell B G. Nucleotide sequence of 5S-ribosomal RNA from Escherichia coli. Nature 1967;215(5102):735-6.

36. Brownlee G G; Sanger F. Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. Journal of molecular biology 1967;23(3):337-53.

37. Sanger F; Brownlee G G; Barrell B G. A two-dimensional fractionation procedure for radioactive nucleotides. Journal of molecular biology 1965;13(2):373-98.

38. MARCKER K; SANGER F. N-FORMYL-METHIONYL-S-RNA. Journal of molecular biology 1964;8():835-40.

39. Glazer A N; Sanger F. The iodination of chymotrypsinogen. The Biochemical journal 1964;90(1):92-8.

40. Milstein C; Sanger F. An amino acid sequence in the active centre of phosphoglucomutase. The Biochemical journal 1961;79():456-69.

41. Naughton M A; Sanger F. Purification and specificity of pancreatic elastase. The Biochemical journal 1961;78():156-63.

42. Naughton M A; Sanger F; Hartley B S; Shaw D C. The amino acid sequence around the reactive serine residue of some proteolytic enzymes. The Biochemical journal 1960;77():149-63.

43. Sanger F; Shaw D C. Amino-acid sequence about the reactive serine of a proteolytic enzyme from Bacillus subtilis. Nature 1960;187():872-3.

44. Sanger F. Chemistry of insulin. British medical bulletin 1960;16():183-8.

45. Milstein C; Sanger F. The amino acid sequence around the serine phosphate in phosphoglucomutase. Biochimica et biophysica acta 1960;42():173-4.

46. Hartley B S; Naughton M A; Sanger F. The amino acid sequence around the reactive serine of elastase. Biochimica et biophysica acta 1959;34():243-4.

47. Sanger F. Chemistry of insulin; determination of the structure of insulin opens the way to greater understanding of life processes. Science (New York, N.Y.) 1959;129(3359):1340-4.

48. Williams J; Sanger F. The grouping of serine phosphate residues in phosvitin and casein. Biochimica et biophysica acta 1959;33(1):294-6.

49. Harris J I; Naughton M A; Sanger F. Species differences in insulin. Archives of biochemistry and biophysics 1956;65(1):427-38.

50. Brown H; Sanger F; Kitai R. The structure of pig and sheep insulins. The Biochemical journal 1955;60(4):556-65.

51. Ryle A P; Sanger F; Smith L F; Kitai R. The disulphide bonds of insulin. The Biochemical journal 1955;60(4):541-56.

52. Ryle a p; Sanger F. Disulphide interchange reactions. The Biochemical journal 1955;60(4):535-40.

53. Sanger F; Thompson E O; Kitai R. The amide groups of insulin. The Biochemical journal 1955;59(3):509-18.

54. Sanger F; Smith L F; Kitai R. The disulphide bridges of insulin. The Biochemical journal 1954;58(330th Meeting):vi-vii.

55. Ryle A P; Sanger F. Disulphide interchange reactions. The Biochemical journal 1954;58(330th Meeting):v-vi.

56. Sanger F. A disulphide interchange reaction. Nature 1953;171(4362):1025-6.

57. Sanger F; Thompson E O P. The amino-acid sequence in the glycyl chain of insulin. II. The investigation of peptides from enzymic hydrolysates. The Biochemical journal 1953;53(3):366-74.

58. Sanger F; Thompson E O P. The amino-acid sequence in the glycyl chain of insulin. I. The identification of lower peptides from partial hydrolysates. The Biochemical journal 1953;53(3):353-66.

59. Sanger F; Thompson E O P. The amino-acid sequence in the glycyl chain of insulin. The Biochemical journal 1952;52(1):iii.

60. Sanger F. The arrangement of amino acids in proteins. Advances in protein chemistry 1952;7():1-67.

61. Sanger F; Thompson E O P. The inversion of a dipeptide sequence during hydrolysis in dilute acid. Biochimica et biophysica acta 1952;9(2):225-6.

62. Sanger F; Tuppy H. The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. The Biochemical journal 1951;49(4):481-90.

63. Sanger F; Tuppy H. The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates. The Biochemical journal 1951;49(4):463-81.

64. Bailey K; Sanger F. The chemistry of amino acids and proteins. Annual review of biochemistry 1951;20():103-30.

65. Sanger F. Some chemical investigations on the structure of insulin. Cold Spring Harbor symposia on quantitative biology 1950;14():153-60.

66. Sanger F. Fractionation of oxidized insulin. The Biochemical journal 1949;44(1):126-8.

67. Sanger F. The terminal peptides of insulin. The Biochemical journal 1949;45(5):563-74.

68. Sanger f. Some peptides from insulin. Nature 1948;162(4117):491.

69. Porter r r; sanger f. The free amino groups of haemoglobins. The Biochemical journal 1948;42(2):287-94.

70. Porter R R; Sanger F. The free amino groups of haemoglobins. The Biochemical journal 1948;42(2):287-94.

71. Sanger F. The free amino group of gramicidin S. The Biochemical journal 1946;40(2):261-2.

72. Sanger F. The free amino groups of insulin. The Biochemical journal 1945;39(5):507-15.

73. Neuberger A; Sanger F. The availability of in-acetyl-d-lysine and in-methyl-dl-lysine for growth. The Biochemical journal 1944;38(1):125-9.

74. Neuberger A; Sanger F. The metabolism of lysine. The Biochemical journal 1944;38(1):119-25.

75. Neuberger A; Sanger F. The availability of the acetyl derivatives of lysine for growth. The Biochemical journal 1943;37(4):515-8.

76. Harris H A; Neuberger A; Sanger F Lysine deficiency in young rats. The Biochemical journal 1943;37(4):508-13.

77. Neuberger A; Sanger F. The nitrogen of the potato. The Biochemical journal 1942;36(7-9):662-71.



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  • Postings

    Head of the Protein Chemistry division
    Laboratory of Molecular Biology Cambridge