Autobiography of Frederick Sanger

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www.worldofchemicals.com

Biography & contributionsFrederick Sanger was born on August 13, 1918 [Died on

November 19, 2013]Sanger was British chemist and double Noble prize

receiverHe extensively worked on proteins like Insulin.Sanger determined base sequences in nucleic acidNucleic acid bases include

                Pyrimidines  – Adenine; Guanine                Purines  – Cytosine; Thymine; Uracil He also worked on ‘recombinant DNA’In 1967 sanger’s team determined sequence of 5S

ribosomal RNA

Frederick Sanger awards list

Awards list1950, Fellow of the Royal Society1951, Corday–Morgan Medal1958, Nobel Prize in chemistry1969, Royal Medal1971, Gairdner Foundation International Award1976, William Bate Hardy Prize1977, Copley Medal1978, G.W. Wheland Award1979, Louisa Gross Horwitz Prize1979, Albert Lasker Award1980, Nobel Prize in chemistry1994, Association of Bimolecular Resource Facilities Award

Recombinant DNARecombinant 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

Recombinant DNA Cont.. In 1977 He proposed Sangers method of dideoxy

chain-termination method for sequencing DNA molecules 

He sequenced insulin proteinInsulinInsulin 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.

Recombinant DNA ProcedureProcedure 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.

Recombinant DNA Procedure Cont..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.