ANFINSEN (Anfinsen), Christian

genus. March 26, 1916
American biochemist Christian Boehmer Anfinsen was born in Monessene (Pennsylvania), a small mill town near Pittsburgh. His father, after whom he was named, immigrated to the U.S. from Norway, and his mother, Sofia Anfinsen (nee Rasmussen), was also of Norwegian descent. At the end of the local school A. entered Svortmor College, where in 1937. he was awarded a bachelor's degree. He then studied organic chemistry at the University of Pennsylvania, while performing duties of assistant teacher of the subject. In 1939, Mr.. He received a Master of Science, and the following year transferred to Carlsberg Laboratory in Copenhagen (Denmark) as a Fellow of the American-Scandinavian Foundation.
Returning in 1940. in the United States, A. receives a scholarship to Harvard University. Three years later, it was he awarded a doctorate in biochemistry, and he became a lecturer in the Department of Biological Chemistry, Harvard Medical School in Boston. In 1944 ... 1946. He serves on the civilian position in the Office of research and development work U.S.. During the 1947/48 academic r. was a junior researcher of the American Cancer Society at the biochemical department of the Nobel Institute in Sweden, where he worked under the guidance of a. Hugo Hugo Theorell. After returning to the U.S. A. became an associate professor at Harvard, . but at the end of the year left the post and headed the laboratory of cellular physiology at the National Institute of Cardiology, . part of the National Board of Health (NHS) in Bethesda (Maryland).,
. In a doctoral dissertation
. described his research to develop methods for measuring the activity of enzymes located in the retina. Enzymes - a chain of amino acids that control chemical reactions in living organisms. Since the enzymes are more catalytic and not structural proteins (similar to muscle proteins), they control the reactions themselves are not engaging in them. When A. began this work, it was known that the chain of amino acids curled in a three-dimensional spherical. It was assumed that each type of protein coiled, although not known how, and takes some, but for him a characteristic shape, which is linked to its function. But nobody at that time had not yet determined the complete amino acid sequence of an enzyme and did not know anything about how enzymes control a huge set of known biochemical reactions.
A. believed that to understand the relationship of structure and function of enzymes necessary to examine the process of collecting them in living organisms. In the mid 40-ies. He and his colleague David Steinberg began to explore the incorporation of amino acids labeled in proteins. Previously, Frederick Sanger at Cambridge University in England has identified the sequence of the 51 th amino acid protein of insulin. Applying the methods of Sanger in their studies, A. suggested that if he synthesizes a chain of amino acids by adding them one by one, and will measure its activity after each stage, he can accurately determine the relationship between the properties of the enzyme and amino acid sequence. For his research he chose ribonuclease bull - an enzyme consisting of 124 amino acids and are synthesized in the pancreas. Splitting the nucleotide chain of ribonucleic acid (RNA) in food, ribonuclease makes it possible to reuse the components in the body of the chain.
. Almost at the same time, the research team the Rockefeller Institute (now Rockefeller University), led by Stanford Moore and William X
. Stein, started work on a similar problem. And Soon. realized that this group can determine the amino acid sequence of the enzyme before it will do it myself.
Rockefeller Prize Awarding allowed A. take a vacation in the NHS and to academic 1954/55 r. a Carlsberg Laboratory, working under the direction of Kai Linderstrema-Lang. As a physical chemist, Linderstrem Lang helped A. in the study of enzymes, 'depriving these organic compounds - as he later wrote a. - These large non-crystalline macromolecules veil of secrecy '. Planning to do only the first synthesis of an enzyme, it nevertheless decided to proceed with the examination of the whole molecule of ribonuclease, watching her in various conditions.
. At that time it was known that proteins denature (lose their activity) in different chemical conditions
. Denaturation occurs when the forces supporting the chain of amino acids (primary structure) in particular, densely packed configuration (tertiary structure), are destroyed by transferring proteins in the disordered state of the coil. One of the factors that support the tertiary structure is the presence of disulfide bonds, bridges are formed between the sulfur-containing amino acid cystine. A. partially unwound ribo-nuclease, denaturing it and chemically destroying it contains four disulfide bonds, to obtain a single randomly twisted (and therefore inactive) chains of amino acids. Then he discovered that when this disordered structure is transferred into the chemical environment that resembles the one in which ribonuclease is located in the body, the initial active tertiary structure is gradually restored.
By 1962, Mr.. A. completed the physical and chemical research, which has demonstrated its 'thermodynamic hypothesis'. In accordance with his view, . tertiary structure of the active ribonuclease formed as a result of the rearrangement of amino acids under physiological conditions, . and this configuration has the lowest energy and, . hence, . is the most stable,
. Only one amino acid sequence determines the tertiary structure of the enzyme and its functional activity.
In 1962. A. left the NHS and became a professor of biochemistry at Harvard Medical School, but next year he returned and led the Laboratory of Chemical Biology at the National Institute of Arthritis, Metabolism and diseases of the digestive system. Here during the 60-ies. he had studied the structural and functional relationships of many proteins. Realizing that can simplify their work, using an enzyme that does not contain disulfide bonds, A. investigated nuclease molecule from the bacterium Staphylococcus aureus. By 1970, Mr.. enzyme was finally synthesized by researchers at Rockefeller University.
'For the work on the study of ribonuclease, especially the relationship between the amino acid sequence and its biologically active konfermentami', A. was awarded half the Nobel Prize in Chemistry for 1972. Moore and Stein shared the second part of the premiums for the same work. In a speech at the presentation of a member of the Royal Swedish Academy of Sciences Po G. MalmstrцІm congratulated the three laureates, who were armed by other researchers 'approach to address the problems of enzyme activity at the molecular level'. MalmstrцІm said that a special interest. focused on the mechanism responsible for the configuration of the peptide chain. 'In a series of elegant experiments he showed that the information is enclosed in a linear sequence of amino acids of the peptide chains that no additional genetic information, greater than that which is contained in DNA is not required'.
. After receiving the Nobel Prize A
. interested interferon - a protein that plays a key role in protecting the body against viruses and cancer. After selecting the substance he took a series of studies on its structure and properties. In 1982, Mr.. he gets the post of professor of biology at Johns Hopkins University.
In 1941, Mr.. A. married Florence Bernays Kenendzher; they have three children - two daughters and a son. In 1978. they divorced.
The following year, A. married Libby Esther Shulman-Eli. In his spare time he is engaged in sailing and listening to music.
A. a member of the Board Weizmann Institute of Science in Rehovot (Israel) and a member of the American Society of Biochemistry, U.S. National Academy of Sciences and the Royal Danish Academy of. In 1954, Mr.. he won the civil service of the Rockefeller Foundation. He was awarded honorary degrees Sortmor College, Providence College, New York Medical College, and Georgetown. Pennsylvania and Bransdeyskogo universities.