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Discreet Charm of Protein Binding Sites
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MORE ABOUT THIS BOOK

Main description:

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.


Feature:

Covers the great discoveries of protein crystallography of the 20th century, as told by one of the protagonists

Explains the unique selectivity of proteins in the binding of small molecules

Addresses the most important questions about protein binding sites


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.


Contents:

Introduction.- Tubulin.- A variety of saccharide binding-sites.- The secret of protein sophistication.- Curious binding-sites – in membrane transport proteins.


PRODUCT DETAILS

ISBN-13: 9783319249964
Publisher: Springer (Springer International Publishing)
Publication date: December, 2015
Pages: 100

Subcategories: Biochemistry

MEET THE AUTHOR

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 solution of its structure.