Frederick Sanger double Noble prize winner works, contribution chemistry

Frederick Sanger – Double Nobel prize winner

Category : Personalities
Published by : Data Research Analyst, Worldofchemicals.com

Biography & contributions

Frederick Sanger was born on August 13, 1918 - Died on November 19, 2013.Sanger was British chemist and double Noble prize receiver

Awards list

1950, Fellow of the Royal Society

1951, Corday–Morgan Medal

1958, Nobel Prize in chemistry

1969, Royal Medal

1971, Gairdner Foundation International Award

1976, William Bate Hardy Prize

1977, Copley Medal

1978, G.W. Wheland Award

1979, Louisa Gross Horwitz Prize

1979, Albert Lasker Award

1980, Nobel Prize in chemistry

1994, Association of Bimolecular Resource Facilities Award

He extensively worked on proteins like Insulin.Sanger determined base sequences in nucleic acid

Nucleic acid bases include

He also worked on ‘recombinant DNA’

In 1967 sanger’s team determined sequence of 5S ribosomal RNA

Recombinant DNA

Recombinant DNA or rDNA is a class of artificial DNA that is created by combining two or more sequences.Peter Lobban was the first person introduce the recombinant DNA technology

Recombinant DNA technology was made possible by the discovery, isolation and application of restriction endonucleases.In 1964 Sanger discovered other class of RNA I.e., tRNA

In 1977 He proposed Sangers method of dideoxy chain-termination method for sequencing DNA molecules.He sequenced insulin protein

Insulin

Insulin is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, skeletal muscles, and fat tissue to absorb glucose from the blood.In the year of 1951 & 1952 Sanger determine the complete amino acid sequence of the two polypeptide chains of bovine insulin A and B.

Procedure

Sanger proved that proteins have a outlined chemical composition. For this method he used Sanger reagent or 1-Fluoro-2,4-dinitrobenzene [FDNB ] to react with the exposed N-terminal amino group at one end of the polypeptide chain. He then partially hydrolyzed the insulin into short peptides, either with hydrochloric acid or using an enzyme such as trypsin.

The mixture of peptides was fractionated in two dimensions on a sheet of filter paper, first by electrophoresis in one dimension and then, perpendicular to that, by chromatography in the other. The different peptide fragments of insulin, detected with ninhydrin, moved to different positions on the paper, creating a distinct pattern called fingerprints.

The peptide from the N-terminus could be recognized by the yellow colour imparted by the FDNB label and the identity of the labelled amino acid at the end of the peptide determined by complete acid hydrolysis and discovering which dinitrophenyl-amino acid was there. By repeating this type of procedure Sanger was able to determine the sequences of the many peptides generated using different methods for the initial partial hydrolysis.

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