He was an American biochemist who won the Nobel Prize for his pioneering work on the structure of enzymes and the relationship between enzyme functions and amino acid sequence.
US biochemist. He studied the relationship between the molecular structures of proteins and their functions. He was born on March 26, 1916, in Monessen, Pennsylvania. After studying at Swarthmore College and the University of Pennsylvania, he received his Ph.D. in biochemistry from Harvard University in 1943. Since then, he has worked as a researcher and lecturer in organic chemistry and biochemistry at the same university and at research institutes in various cities in Europe. Between 1947 and 1948, he participated in cancer research conducted by H Theorell at the Nobel Institute in Stockholm. He became a professor of biochemistry at Harvard Medical School in 1962. He was head of the biochemistry laboratory of the National Institute of Arthritis, Metabolism and Digestive Diseases in the USA when he won the 1972 Nobel Prize in chemistry. In 1982 he was appointed professor of biology at Johns Hopkins University.
Anfinsen first started his studies on the molecular structure of proteins with an enzyme secreted by the gastric mucosa; because this enzyme, known as “pepsin”, was one of the first types of protein to be obtained in pure form. He then set about deciphering the structure of an enzyme called "ribonuclease," which hydrolyzes RNA (ribonucleic acid). In the 1950s, about twenty years before sharing the Nobel Prize with Stein and Moore, he succeeded in separating the disulfide bonds (-S-S) that connect the amino acids in the structure of this enzyme, which consists of 124 amino acids, into two sulfhydryls (-SH) groups by reduction method. According to Anfinsen's observations, this reduction could not occur under normal environmental conditions and required high temperature and high pH (alkaline environment). Moreover, the enzyme, which lost its active structure (denatured) as a result of such reduction, could regain its former structure and function by oxidation by binding the oxygen in the air under certain conditions. Anfinsen thought that the inability of an enzyme to perform its function in its natural molecular arrangement when it is denatured can only be explained by a coding present in the structure of the molecular chain. As a matter of fact, these findings, which were supported and generalized by studies on other proteins, formed the basis for genetic and biochemistry studies, which intensified in the following years, in terms of emphasizing the relationship between the structure and functions of molecular chains.
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Christian Anfinsen - Facts
https://www.nobelprize.org/prizes/chemistry/1972/anfinsen/biographical/