Structural Biochemistry/John C. Kendrew

Introduction
John Cowdery Kendrew (March 24, 1917 - Aug. 23, 1997) was an English biochemist who was awarded the Nobel Prize in Chemistry in 1962 for his work for pioneering the use of x-ray crystallography in determining protein structure and more specifically the structure of myoglobin.

Biography
Kendrew was born in Oxford, England to a Wilfred George Kendrew and Evelyn May Graham Sandberg. He obtained a BS in Chemistry at Trinity College in 1939 and later obtained his PhD also at Trinity College in 1949. After his BS, Kendrew researched on reaction kinetics in the Department of Physical Chemistry at Cambridge. As time progressed, his interests slowly became more biological and eventually he decided to work on the structure of proteins. In 1946, he met his future colleague with whom he'd later share his Nobel Prize with, Max F. Perutz, in the Cavendish Laboratory, the Department of Physics at the University of Cambridge.

Nobel Prize in Chemistry (1962)
The 1962 Nobel Prize in Chemistry was awarded to not only Kendrew, but also to his colleague Max F. Perutz for their achievement in successfully using X-rays to determine the structures of complex proteins. While x-ray crystallography at the time could be used to determine the structure of simple compounds with tens of atoms, it was unable to do the same for complex structures because it was near impossible to know which phase, the point in the cycle of waves, the X-rays were at when they formed a dot. Perutz solved this problem with the use of heavy atoms, more specifically mercury, and putting them into specific positions in a protein molecule. The atoms altered the intensity of the diffraction pattern in a manner allowing them to determine the location of the atoms which provided a reference point used to calculate the missing phase information. Perutz then used this method to determine the structure of hemoglobin, while Kendrew used this method to determine the structure of myoglobin.