Christian Boehmer Anfinsen (26 March 1916 – 14 May 1995) was an American biochemist who was awarded the Nobel Prize in Chemistry in 1972 for his work on the relationship between the chemical structure and the biological activity of proteins.
Life and Career
He was born on 26 March 1916, in Monessen, Pennsylvania, US. He earned his undergraduate degree in chemistry in 1937, from Swarthmore College. Then, he enrolled at the University of Pennsylvania, where he earned his Ph.D. in biochemistry in 1941.
His most famous experiment involved the protein ribonuclease, which he showed could be denatured by breaking the disulfide bonds that held its folded structure together. When the disulfide bonds were re-formed, the protein spontaneously refolded into its native structure and regained its biological activity. This demonstrated that the information needed to specify the protein’s structure was contained within its amino acid sequence.
Anfinsen’s work had profound implications for the field of biochemistry and led to a greater understanding of the relationship between the structure and function of proteins. His research also had practical applications, such as in the development of protein-based drugs and in the study of diseases caused by protein misfolding.
Christian Boehmer Anfinsen died on 14 May 1995, in Randallstown, Maryland, US.
Award and Legacy
He received the Nobel Prize in Chemistry in 1972 for his work on the relationship between the chemical structure and the biological activity of proteins.
His legacy continues to inspire researchers in the fields of biochemistry and molecular biology. His pioneering work on protein folding has led to the development of new drugs and therapies for a wide range of diseases, and his research has helped to establish the fundamental principles that govern the behavior of proteins in cells.
Anfinsen’s contributions to science have had a profound impact on our understanding of the molecular basis of life, and his legacy continues to inspire new generations of scientists.