Kendrew, John

Kendrew,John. The Thread of Life. Cambridge, Mass. Harvard University Press, 1966. 

K (symbol for equihbrium constant) relation to AG°, 106—107 Karplus, Martin, 544 Kazan, University of, 3 Kekule, August, 3, 399-402 Kendrew, John C., 1087 a-Keratin, 1085 Ketals. See Acetals Ketene, 783... 

For their work on myoglobin and hemoglobin respec tively John C Kendrew and Max F Perutz were awarded the 1962 Nobel Prize in chemistry... 

In small-molecule crystallography the phase problem was solved by so-called direct methods (recognized by the award of a Nobel Prize in chemistry to Jerome Karle, US Naval Research Laboratory, Washington, DC, and Herbert Hauptman, the Medical Foundation, Buffalo). For larger molecules, protein aystallographers have stayed at the laboratory bench using a method pioneered by Max Perutz and John Kendrew and their co-workers to circumvent the phase problem. This method, called multiple isomorphous replacement... 

Proteins are complex molecules, typically containing several thousand atoms. Although Pauling and Corey proposed the a helix and the 3 sheet as the main secondary structural elements of proteins in 1951, and the crystal structure of myoglobin was reported by John Kendrew in 1958,... 

A brief look at the contents page of any recent issue of the Journal of Molecular Biology (founded by John Kendrew, protein crystallographer and winner of the Nobel Prize for Chemistry together with Max Perutz for the 3-D structures of myoglobin and haemoglobin) will clearly establish that this is not so. 

Haemoglobin is one of the most well studied and best understood proteins thanks largely to the early work of Max Perutz, John Kendrew and colleagues. Haemoglobin is now often used as a model allosteric protein and to illustrate the impact of protein structural alterations in disease. 

The Encyclopedia of Molecular Biology (1994) edited by John Kendrew. Blackwell Science. 

John Kendrew found that the x-ray diffraction pattern of crystalline myoglobin (isolated from muscles of the sperm whale) is very complex, with nearly 25,000 reflections. Computer analysis of these reflections took place in stages. The resolution improved at each stage, until in 1959 the positions of virtually all the non-hydrogen atoms in the protein had been determined. The amino acid sequence of the protein, obtained by chemical analysis, was consistent with the molecular model. The structures of thousands of proteins, many of them much more complex than myoglobin, have since been determined to a similar level of resolution. 

John C. Kendrew and Max F. Perutz Chemistry Structures of protein by X-ray diffraction... 

The elucidation of the structure of ribonuclcasc follows that of lycozyme by a group at London s Royal Institute headed by Dr. David C. Phillips, and that of the other protein, myoglobin, for which Dr. Max F. Perutz and Dr. John C. Kendrew of Cambridge University received the Nobel Prize in chemistry in 1962. 

PERUTZ. MAX F. (1914-2002). An Austrian molecular biologist and recipient of the Nobel prize for chemistry in 1962 along with John C. Kendrew, His work was concerned with crystalline protein structure, particularly the molecular structure of hemoglobin and myoglobin. His education was in England and Austria. 

---