تسجيل الدخول

تسجيل

The Covalent Structure of Proteins:-The Amino Acid Sequences of Millions of Proteins Have Been Determined

المؤلف:  David L. Nelson، Michael M. Cox

المصدر:  Lehninger Principles of Biochemistry

الجزء والصفحة:  p96-97

2026-04-15

522

The Covalent Structure of Proteins:-The Amino Acid Sequences of Millions of Proteins Have Been Determined

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 sequence of DNA in determining the amino acid sequence of protein molecules was revealed (Chapter 27). An enormous number of protein sequences can now be derived indirectly from the DNA sequences in the rapidly growing genome databases. However, many are still deduced by traditional methods of polypeptide sequencing. The amino acid sequences of thousands of different proteins from many species have been determined using principles first developed by Sanger. These methods are still in use, although with many variations and improvements in detail. Chemical protein sequencing now complements a growing list of newer methods, providing multiple avenues to obtain amino acid sequence data. Such data are now critical to every area of bio chemical investigation.

FIGURE 3–24 Amino acid sequence of bovine insulin. The two polypeptide chains are joined by disulfide cross linkages. The A chain is identical in human, pig, dog, rabbit, and sperm whale insulins. The B chains of the cow, pig, dog, goat, and horse are identical.