Frederick Sanger was a British chemist who received two Nobel Prizes for his work determining the structures of proteins like insulin and nucleic acids like RNA. He developed methods for sequencing proteins and DNA that enabled the discovery of gene sequences and advanced recombinant DNA technology. Sanger determined the complete amino acid sequences of insulin and sequenced the first RNA. His sequencing methods revolutionized molecular biology and helped launch the biotechnology industry.
2. Biography & contributions
Frederick Sanger was born on August 13, 1918 [Died on
November 19, 2013]
Sanger was British chemist and double Noble prize receiver
He extensively worked on proteins like Insulin.
Sanger determined base sequences in nucleic acid
Nucleic 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
3. Frederick Sanger awards list
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
4. 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
5. Recombinant DNA Cont..
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.
6. Recombinant DNA Procedure
Procedure
Sanger proved that proteins have a outlined chemical
composition. For this method he used Sanger reagent or 1Fluoro-2,4-dinitrobenzene [FDNB ] to react with the exposed Nterminal 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.
7. 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.