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Chemist Profiles

Frederick Sanger

1918–2013

The quiet biochemist who read the sequence of a protein, then of DNA, and won two Nobel Prizes in Chemistry.

Last reviewed 5 October 2026

Who he was

Frederick Sanger was born in a small English village and studied at the University of Cambridge, where he spent his entire career. He described himself as “just a chap who messed about in a lab”, yet he solved two of the great problems of twentieth-century chemistry: the order of the building blocks in proteins, and then in DNA.

Key contributions

The sequence of insulin. In the 1940s nobody knew whether a protein had a definite sequence of amino acids. Sanger broke insulin into small fragments, labelled the end amino acid of each fragment with a coloured reagent, separated the fragments by paper chromatography and electrophoresis, and pieced the overlaps together like a jigsaw. After about ten years, in 1955, he had the complete sequence: two chains of 21 and 30 amino acids, joined by disulfide bridges.

Key idea

Insulin proved that every protein has one exact sequence of amino acids, written into the cell by its genes. A protein is a polymer, but unlike polythene it is not a random chain: the order of its monomers is everything.

Reading DNA. Sanger then turned to DNA. His chain-termination method (1977) copies a DNA strand with an enzyme, using a small amount of special nucleotides that stop the copy at each A, C, G or T. Sorting the stopped copies by length reads the sequence base by base. With it his group read the first complete genome, of a virus about 5400 bases long. Improved versions of the method were used to read the human genome, completed in 2003.

Prizes and legacy

He won the 1958 Nobel Prize in Chemistry for the structure of insulin and shared the 1980 Nobel Prize in Chemistry for DNA sequencing. He was the first person to win the chemistry prize twice. He declined a knighthood because he did not want to be called “Sir”, but accepted the Order of Merit in 1986.

Connections to your lessons

His work brings together the lessons on chromatography (separating fragments), functional groups (amino and carboxyl groups forming peptide links) and polymers (proteins and DNA as natural polymers).

Timeline

  1. 1918Born in Rendcomb, England; his father, a doctor, brings up his sons as Quakers.
  2. 1943Earns his PhD at the University of Cambridge, where he stays for the rest of his career.
  3. 1945Introduces a reagent (fluorodinitrobenzene) that labels the amino acid at the end of a protein chain.
  4. 1955Completes the full amino acid sequence of insulin: two chains, of 21 and 30 amino acids, linked by sulfur bridges.
  5. 1958Awarded the Nobel Prize in Chemistry for the structure of proteins, especially insulin.
  6. 1962Moves to the new MRC Laboratory of Molecular Biology in Cambridge and turns to nucleic acids.
  7. 1977Publishes the chain-termination (dideoxy) method and the first complete DNA genome, of the virus phi X 174, about 5400 bases long.
  8. 1980Shares the Nobel Prize in Chemistry for methods of sequencing DNA, becoming the first person to win the chemistry prize twice.
  9. 1983Retires and spends his time gardening.
  10. 1993The Sanger Centre (now the Wellcome Sanger Institute), a leading genome research centre, is named after him.
  11. 2013Dies in Cambridge, aged 95.

Sources and further reading

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