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The Discreet Charm of Protein Binding Sites

by Joseph Yariv
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Current price ₹3,672.00
Original price ₹5,649.00
Original price ₹5,649.00
Original price ₹5,649.00
(-35%)
₹3,672.00
Current price ₹3,672.00

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Book cover type: Hardcover
  • ISBN13: 9783319249940
  • Binding: Hardcover
  • Subject: N/A
  • Publisher: Springer
  • Publisher Imprint: Springer
  • Publication Date:
  • Pages: 60
  • Original Price: EUR 49.99
  • Language: English
  • Edition: 2016
  • Item Weight: 286 grams
  • BISAC Subject(s): Life Sciences / Biochemistry, Physics / Crystallography, and Life Sciences / Biophysics

From the Back Cover
This book is a passionate account of the scientific breakthroughs that led to the solution of the first protein structures and to the understanding of their function at atomic resolution. The book is divided into self-standing chapters that each deal with a protein or protein family. The subject is presented in a fluid, non-technical style that will engage student and scientists in biochemistry, biophysics, molecular and structure biology and physiology.

Joseph Yariv graduated from The Hebrew University in Jerusalem with a Ph.D. in biochemistry. After postdoctoral studies at the Sloan Kettering Institute and Columbia University in New York, USA he joined the department of biophysics of The Weizmann Institute of Science in Rehovot, Israel where he worked until his retirement in the position of Senior Scientist. His work dealt with protein isolation, crystallization and structure solution. He was the first to label a methionine in the active-site of b-galacosidase of E. coli. He produced crystals of concanavalin A complexes with methyl-glucoside and with methyl-mannoside and participated in solving the structure of this protein binding-site for saccharides. He collaborated with physicists at The Hebrew University in Jerusalem in studying by Mossbauer Spectroscopy the state of iron in E. coli that led to the isolation of bacterioferritin, the first ferritin-like molecule to be found in bacteria and named as such, and solutionof its structure.

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