Frederick Sanger

At 95 years old, Frederick Sanger physical status not available right now. We will update Frederick Sanger's height, weight, eye color, hair color, build, and measurements.

Research and career

Neuberger left Cambridge for the National Institute for Medical Research, but Sanger remained in Cambridge and joined Charles Chibnall, a protein chemist who had recently taken up the chair in the Department of Biochemistry. Chibnall had already done some research into bovine insulin's amino acid composition, and had suggested that Sanger investigate the protein's amino acid compositions. Insulin was available from Boots, and it was one of the few proteins that were in a pure form. Sanger had been investing himself up to this point. He was first sponsored by the Medical Research Council and then by a Beit Memorial Fellowship for Medical Research from 1944 to 1951 in Chibnall's group.

Sanger's first victory was to determine the complete amino acid sequence of the two polypeptide chains of bovine insulin, A and B, in 1952 and 1951, respectively. Proteins were traditionally thought to be somewhat amorphous prior to this. Sanger established that proteins had a defined chemical composition when determining these sequences.

Sanger refined a partition chromatography technique first developed by Richard Laurence Millington Synge and Archer John Porter Martin to determine amino acids in wool. Sanger used a chemical reagent 1-fluoro-2,4-dinitrobenzene (now known as Sanger's reagent, fluorodinitrobenzene, FDNB or DNFB), which was obtained from toxic gas research conducted by Bernhard Saunders at Cambridge University's Chemistry Department. The reagent used by Sanger was particularly effective at identifying the N-terminal amino group at one end of the polypeptide chain. He converted the insulin partially hydrolysed insulin into short peptides, either with hydrochloric acid or an enzyme such as trypsin. The peptide mixture was fractionated in two dimensions on a sheet of filter paper, first by electrophoresis in one direction and then chromatography in the other. The different peptide fragments of insulin, which had been analyzed with ninhydrin, rose to different positions on the paper, resulting in a distinctive pattern that Sanger referred to as "fingerprints." The peptide from the N-terminus could be identified by the yellow color provided by the FDNB label and the identity of the labelled amino acid at the end of the peptide analysis, which determined which dinitrophenyl-amino acid was present and determining which dinitrophenyl-amino acid was present.

Sanger was able to determine the sequences of the many peptides obtained by different methods of initial partial hydrolysis by repeating this procedure. These could then be assembled in longer sequences to obtain insulin's complete structure. Finally, because the A and B chains are physiologically inactive without the three separating disulfide bonds (two interchain, one intrachain on A), Sanger and coworkers selected their positions in 1955. Sanger's main conclusion was that the two polypeptide chains of the protein insulin were controlled amino acid sequences and, by extension, that each protein had a unique sequence. In 1958, it was this achievement that earned him his first Nobel Prize in Chemistry. This finding was pivotal for Crick's later sequence hypothesis of how DNA codes for proteins.

Sanger, a 1951 graduate of the Medical Research Council's externer, and the institution's Laboratory of Molecular Biology was opened in 1962, he moved from his Biochemistry Department to the top floor of the new building. He took over the Protein Chemistry group.

Sanger began investigating the possibility of sequencing RNA molecules and figuring out techniques for separating ribonucleotide fragments that were created with specific nucleases ahead of his transfer. He performed this work while trying to refine the sequencing techniques he had developed during his insulin research.

The primary challenge in the research was to sequence a single piece of RNA. He discovered the formylmethione tRNA, which stimulates protein synthesis in bacteria, in the course of his research in 1964. He was disqualified in the competition to sequence a tRNA molecule by a Cornell University group led by Robert Holley, who published the sequence of the 77 ribonucleotides of Saccharomyces cerevisiae in 1965. Sanger's group had established the nucleotide sequence of the 5S ribosomal RNA from Escherichia coli, a small RNA with 120 nucleotides by 1967.

Sanger then turned to sequencing DNA, which would require a completely different approach. He investigated various ways to copy single stranded DNA from E. coli to produce single stranded DNA. He developed the "Plus and Minus" method in 1975, along with Alan Coulson, and developed a sequencing technique using DNA polymerase with radiolabeled nucleotides. Two closely related methods were used to produce short oligonucleotides with defined 3' termini. Electrophoresis on a polyacrylamide gel could reduce the quantities and be visualized by autoradiography. The procedure could be repeated in a single step and was a major improvement on what had been used before, but it was still laborious. Despite this, his team was able to sequence the majority of the 5,386 nucleotides of the single-stranded bacteriophage X174. This was the first fully sequenced DNA sequenced genome. The gene locators of some of the genes were found to match one another, much to their surprise.

The "dideoxy" chain-termination method for sequencing DNA molecules, also known as the "Sanger technique," was introduced by Sanger and colleagues in 1977. This was a big breakthrough, because DNA was able to be sequenced for long stretches of DNA. In 1980, he shared with Walter Gilbert and Paul Berg his second Nobel Prize in Chemistry, which he shared with Walter Gilbert and Paul Berg. Sanger and colleagues were able to sequence human mitochondrial DNA (16,569 base pairs) and bacteriophage bacteriophage (16,502 base pairs). The dideoxy technique was eventually used to sequence the complete human genome.

During his career, Sanger mentored more than ten PhD students, two of whom went on to win Nobel Prizes. Rodney Porter, the company's first graduate student, joined the faculty in 1947. Porter later received the Nobel Prize in Physiology or Medicine from Gerald Edelman for his research on antibodies' chemical structure. Elizabeth Blackburn obtained a PhD in Sanger's laboratory between 1971 and 1974. Carol W. Greider and Jack W. Szostak received the 2009 Nobel Prize in Physiology or Medicine for her research into telomeres and the development of telomerase.

This decision should not be confused with Terence Sanger's ruling, which is linked to Oja's reign.

Sanger is one of the only two Nobel Laureates in Chemistry to have been awarded twice (the other being Karl Barry Sharpless in 2001 and 2022), John Bardeen (Chemistry, 1954 and 1972), and Karl Barry Sharpless (twice Chemistry, 2001 and 2002).

In his honour, the Wellcome Trust Sanger Institute (formerly the Sanger Centre) has been named in his honour.

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