Anfinsen

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Anfinsen

The term "Anfinsen" primarily refers to Christian B. Anfinsen, an influential American biochemist who was awarded the Nobel Prize in Chemistry in 1972 for his work on ribonuclease and the principles that govern protein folding. His research has had a profound impact on the field of biochemistry and molecular biology.

Biography[edit | edit source]

Christian Boehmer Anfinsen was born on March 26, 1916, in Monessen, Pennsylvania, USA. He pursued his undergraduate studies at Swarthmore College, where he graduated with a Bachelor of Science degree in chemistry in 1937. Anfinsen continued his education at the University of Pennsylvania, earning a Master of Science degree in organic chemistry in 1939. He then completed his Ph.D. in biochemistry at Harvard University in 1943.

Scientific Contributions[edit | edit source]

Anfinsen is best known for his groundbreaking work on the folding of proteins, particularly ribonuclease. His research demonstrated that the primary sequence of amino acids in a protein determines its three-dimensional structure, a concept now known as the "Anfinsen's dogma" or "thermodynamic hypothesis."

Anfinsen's Experiment[edit | edit source]

Anfinsen's most famous experiment involved the enzyme ribonuclease A. He showed that when ribonuclease A is denatured and then allowed to refold, it regains its enzymatic activity. This experiment provided strong evidence that the information required for protein folding is contained within the amino acid sequence itself.

Nobel Prize[edit | edit source]

In 1972, Anfinsen was awarded the Nobel Prize in Chemistry, which he shared with Stanford Moore and William H. Stein. The award recognized his work on the connection between the amino acid sequence of a protein and its biologically active conformation.

Legacy[edit | edit source]

Anfinsen's work laid the foundation for the modern understanding of protein folding and stability. His insights have been crucial in the development of fields such as structural biology and bioinformatics. The principles he established continue to guide research in protein engineering and the study of diseases related to protein misfolding.

Also see[edit | edit source]

Template:Nobel laureates in Chemistry

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