John Cowdery Kendrew determined first atomic structures of proteins

John Cowdery Kendrew – determined myoglobin structure

Article on John Cowdery Kendrew

Biography & Contributions

John Cowdery Kendrew was an English biochemist, crystallographer and Noble laureate born on March 24, 1917 – died on August 23, 1997. Kendrew determined the structure of myoglobin

In 1945 he approached Dr. Max Perutz in the Cavendish Laboratory in Cambridge. Kendrew shared the 1962 Nobel Prize for chemistry with Max Perutz for determining the first atomic structures of proteins using X-ray crystallography. Their work was done at what is now the MRC Laboratory of Molecular Biology in Cambridge.

Kendrew determined the structure of the protein myoglobin, which stores oxygen in muscle cells. Kendrew embarked on the study of myoglobin, a molecule only a quarter the size of the hemoglobin molecule. His initial source of raw material was horse heart, but the crystals thus obtained were too small for X-ray analysis. Kendrew realized that the oxygen-conserving tissue of diving mammals could offer a better prospect.

Myoglobin Chemistry

Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. In humans, myoglobin is only found in the bloodstream after muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood.

Myoglobin contains hemes, pigments responsible for the color of red meat. The color that meat takes is partly determined by the degree of oxidation of the myoglobin. In fresh meat the iron atom is the ferrous (+2) oxidation state bound to an oxygen molecule (O2). Meat cooked well done is brown because the iron atom is now in the ferric (+3) oxidation state, having lost an electron. If meat has been exposed to nitrites, it will remain pink because the iron atom is bound to NO, nitric oxide.

Myoglobin belongs to the globin super family of proteins, and as with other globins, consists of eight alpha helices connected by loops.

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