This section contains 1,965 words (approx. 7 pages at 300 words per page) |
World of Chemistry on Max Perutz
Max Perutz pioneered the use of X-ray crystallography to determine the atomic structure of proteins by combining two lines of scientific investigation--the physiology of hemoglobin and the physics of X-ray crystallography. His efforts resulted in his sharing the 1962 Nobel Prize in chemistry with his colleague, biochemist John Kendrew. Perutz's work in deciphering the diffraction patterns of protein crystals opened the door for molecular biologists to study the structure and function of enzymes--specific proteins that are the catalysts for biochemical reactions in cells. Known for his impeccable laboratory skills, Perutz produced the best early pictures of protein crystals and used this ability to determine the structure of hemoglobin and the molecular mechanism by which it transports oxygen from the lungs to tissue. A passionate mountaineer and skier, Perutz also applied his expertise in X-ray crystallography to the study of glacier structure and flow.
Perutz was born in Vienna, Austria...
This section contains 1,965 words (approx. 7 pages at 300 words per page) |