Methods in Enzymology Vol.114 Diffraction Methods for Biological Macromolecules, Part A

In the 1930s, when biochemists began to realize that all chemical reactions in living cells are catalyzed by enzymes, the secret of life was widely believed to lie hidden in the structure of proteins. In earlier times these had been regarded as colloids of indefinite structure, and experiments on gelatin, looked upon as a model of a typical protein, had been a favorite sport among physical chemists with a biological bent. The idea that enzymatic catalysis or oxygen transport might be understood in stereochemical terms seemed utopian. This outlook began to change slowly after the first enzyme, urease, had been crystallized by Sumner in 1928, followed soon afterward by Northrop and Herriott's crystallization of pepsin, trypsin, and chymotrypsin. Early X-ray crystallographers did try to take diffraction pictures of dried crystals of hemoglobin and other proteins, but their weak X-ray patterns were covered up by large backstops or obscured by air scattering.

• Hardcover: 588 pages
• Publisher: Academic Press; 1 edition (December 12, 1985)
• Language: English
• ISBN-10: 0121820149
• ISBN-13: 978-0121820145
• Product Dimensions: 1.2 x 6.2 x 9.2 inches

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