John Kendrew

John Kendrew (1917–1997) was a British biochemist and crystallographer who determined the first atomic structure of a protein, myoglobin. He shared the 1962 Nobel Prize in Chemistry with Max Perutz.

Max Perutz: A British molecular biologist who determined hemoglobin’s structure and shared the 1962 Nobel Prize in Chemistry with John Kendrew. Perutz led the neighboring hemoglobin project at the Cavendish Laboratory and shared Kendrew’s Nobel Prize.
X-ray crystallography: A method for determining atomic arrangements by analyzing how crystals diffract X-rays. This was the experimental foundation of Kendrew’s determination of myoglobin’s structure.
Cavendish Laboratory: A physics laboratory at the University of Cambridge known for influential experimental research. Kendrew’s structural work took place there within Bragg’s research environment.
1962 Nobel Prize in Chemistry: The Nobel Chemistry award shared by Max Perutz and John Kendrew for studies of globular proteins. The prize recognized Kendrew’s and Perutz’s pioneering structural determinations.
Hemoglobin structure: The three-dimensional arrangement of the four protein subunits in hemoglobin. Perutz’s more complex oxygen-transport protein contrasted with Kendrew’s single-chain myoglobin.
Francis Crick: A British molecular biologist who helped discover DNA’s double-helical structure and develop molecular biology. Crick worked alongside Kendrew and Perutz in Cambridge as structural biology took shape.
Protein crystallography: The use of X-ray diffraction from protein crystals to determine protein structures. Kendrew adapted crystallographic methods to solve the structure of a large, complex protein.
MRC Laboratory of Molecular Biology: A Cambridge research institute established to investigate biological structures and processes at the molecular level. Kendrew helped establish the institute that grew from the Cambridge molecular-biology research group.
Protein structure: The three-dimensional arrangement of atoms in a protein molecule. Kendrew’s result supplied the first atomic-level example for a protein.
Nuclear magnetic resonance spectroscopy: A method that uses nuclear magnetic resonance signals to study molecular structure and dynamics. Unlike Kendrew’s crystallographic approach, this method can determine structures without crystals.

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