Sanger, Frederick insulin sequenced

SANGER, FREDERICK (1918—J. A11 English biochemist who won the Nobel prize for cliemistiy ill 1958. His research was on protein structure. He identified the amino acid sequence of the protein insulin. His PhD. was awarded from Cambridge University. 

Frederick Sanger Univ. of sequence determination of insulin... 

The first protein to have its sequence determined by these methods was insulin. This was accomplished in 1953 by the research group headed by Frederick Sanger. Sanger won the 1958 Nobel Prize in chemistry for directing this work. (He also shared the 1980 Nobel Prize for his contributions to DNA sequencing, so he is one of the few individuals to have won two Nobel Prizes.) Sanger chose insulin because it is readily available and is relatively small (51 amino acids). To help see the approach used to solve a problem of this type, let s examine a few of the many experiments that were used. 

Animals ex pancreatic 3 cells discovery (1922) by Frederick Banting, J.B. Collip, Charles Best, J. Macleod (Canada Nobel Prize, Medicine, to Banting MacLeod, 1923) sequence by Fred Sanger (1953) (UK, Nobel Prizes, Chemistry, 1958 [insulin sequence] 1980 [RNA sequencing]) for treatment of Type 1 and advanced Type 2 diabetes mellitus Synthetic... 

Frederick Sanger Chemistry Protein sequencing, insulin... 

The structure and properties of peptides and proteins depend critically upon the sequence of amino acids in the peptide chain. In 1953, Frederick Sanger determined the sequence of the 51 amino acid residues in insulin. The first step in determining the sequence was to ascertain the amino acid composition of insulin,... 

Two major discoveries in 1953 were of crucial importance in the history of biochemistry. In that year James D. Watson and Francis Crick deduced the double-helical structure of DNA and proposed a structural basis for its precise replication (Chapter 8). Their proposal illuminated the molecular reality behind the idea of a gene. In that same year, Frederick Sanger worked out the sequence of amino acid residues in the polypeptide chains of the hormone insulin (Fig. 3-24), surprising many researchers who had long thought that elucidation of the amino acid sequence of a polypeptide would be a hopelessly difficult task. It quickly became evident that the nucleotide sequence in DNA and the amino acid sequence in proteins were somehow related. Barely a decade after these discoveries, the role of the nucleotide... 

The covalent structure of insulin was established by Frederick Sanger in 1953 after a 10-year effort. This was the first protein sequence determination.237 238 Sanger used partial hydrolysis of peptide chains whose amino groups had been labeled by reaction with 2,4-dinitrofluorobenzene239 to form shorter end-labeled fragments. These were analyzed for their amino acid composition and labeled and hydrolyzed again as necessary. Many peptides had to be analyzed to deduce the sequence of the 21-residue and 30-residue chains that are joined by disulfide linkages in insulin.237 238... 

Insulin, the first polypeptide hormone to be identified, was discovered by Frederick G. Banting and Charles Best in 1922. They found that this substance, which they isolated from the pancreas, restored normal glucose utilization in experimental animals lacking a pancreas. Insulin was also the first protein to be sequenced, a landmark accomplishment achieved by Fred Sanger in 1955. About 20 years... 

Frederick Sanger (1918- ) determines the entire sequence of the amino acids in insulin. 

Determining the Amino Acid Sequence of Insulin Figure 3-24 shows the amino acid sequence of the hormone insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. 

In 1953, Frederick Sanger determined the amino acid sequence of insulin, a protein hormone (Figure 3.22). This work is... 

Frederick Sanger in 1953 determined the complete amino acid sequence of insulin for the first time. The important steps involved in determining the primary structure of protein are -... 

Frederick Sanger (1918- ) was born in Gloucestershire, England, and received his Ph.D. at the University of Cambridge in 1943. He was awarded the Nobel Prize in chemistry in 1958 for his determination of the structure of insulin, and in 1980 he became only the fourth person ever to win a second Nobel Prize. This second prize was awarded for his development of a method for sequencing nucleotides in DNA. 

In 19S3, Frederick Sanger determined the amino acid sequence of insulin, a protein hormone (Figure 2.22). This work is a landmark in biochemistry because it showed for the first time that a protein has a precisely defined amino acid sequence consisting only of L amino acids linked by peptide bonds. This accomplishment stimulated other scientists to carry out sequence studies of a wide variety of proteins. Currently, the complete amino acid sequences of more than 2,000,000 proteins are known. The striking fact is that each protein has a unique, precisely defined amino acid sequence. The amino acid sequence of a protein is referred to as its primary structure. 

The importance of insulin made it the focus of Frederick Sanger s work in structural chemistry. Sanger applied chemist Emil Fisher s philosophy, using chemical principles to explicate protein structure and function. Sanger eventually established the order of amino acids that made up insulin, the first protein for which the amino acid sequence was determined. Knowing the sequence enabled comparison between insulins from different species, and discovery of the slight differences between them. 

Insulin was the first protein for which the primary sequence was determined. This was done in 1953 by Frederick Sanger, who received the 1958 Nobel Prize in chemistry for his work. Sanger was bom in England in 1918 and received a Ph.D. from Cambridge University, where he has worked for his entire career. He also received a share of the 1980 Nobel Prize in chemistry (Section 27.15) for being the first to sequence a DNA molecule (with 5375 nucleotide pairs). 

In 1958 Frederick Sanger was awarded his first Nobel Prize in Chemistry for his studies on insulin [1], He had determined its complete amino acid sequence, which proved that proteins have definite stractures. Fifty years later, we have dramatically broadened our understanding of proteins and their role in vivo. Starting from amino acid building blocks, complex proteins have evolved to perform a variety of complex catalytic tasks, hi addition to the amino acid s side chain reactivity. Nature often exploits cofactors and/or metal ions to complement its catalytic repertoire. It is estimated that one third of aU enzymes are metalloproteins and that some of the most difficult biological transformations are mediated by these [2],... 

Probably the most important achievement in insulin research was the determination of its primary structure by Frederick Sanger and his associates in Cambridge, England. In order to elucidate the amino acid sequence of the hormone it was necessary to separate the two chains constituting the molecule. This was accomplished by oxidation with performic acid. This operation cleaved the three disulfide bridges by converting each cystine to two cysteic acid residues ... 

Frederick Sanger discovers the amino acid sequence of insulin. 

Initially amino acids were hard to identify because reaction conditions used by chemists to break up the protein usually destroyed amino acids in the process. But as techniques improved, these units were identified by such chemists as Emil Fischer, Sidney W. Cole, and Frederick Gowland Hopkins. The difficulty was then to decide how amino acids were joined to make up different proteins. In the mid-1940s the first complete analysis of the sequence of amino acids that makes up a protein was achieved. More quickly followed, such as the work by Frederick Sanger in which he unraveled the amino acid sequence for insulin. 

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