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The Discreet Charm of Protein Binding Sites (eBook)

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2015 | 1st ed. 2016
XIII, 60 Seiten
Springer International Publishing (Verlag)
978-3-319-24996-4 (ISBN)

Lese- und Medienproben

The Discreet Charm of Protein Binding Sites - Joseph Yariv
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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 solution of its structure.  

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.  

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

Erscheint lt. Verlag 9.12.2015
Zusatzinfo XIII, 60 p. 16 illus., 10 illus. in color.
Verlagsort Cham
Sprache englisch
Themenwelt Naturwissenschaften Biologie Mikrobiologie / Immunologie
Naturwissenschaften Chemie
Technik
Schlagworte Allosteric Protein • Alpha and Beta Tubulin Dimers • Colchicine Binding-site • Concanavalin A binding Specificity • History of Protein Structure Determination • Human Aquaporins • Membrane Transport Proteins • Protein-Ligand Interactions • Protein Structure by X-ray Crystallography • receptors
ISBN-10 3-319-24996-7 / 3319249967
ISBN-13 978-3-319-24996-4 / 9783319249964
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