Anfinsen
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]
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD