The Discreet Charm of Protein Binding Sites

ISBN-13: 9783319797175 / Angielski / Miękka / 2019 / 60 str.

Joseph Yariv

Opis

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.

Recenzje

"This study is quite probably the inspiration behind 'The discreet charm', which is a personal, and passionate story of how proteins interact with other chemical moieties, be it organic molecules or other proteins. ... The book is well illustrated, both with copies of original figures from the referenced bibliography, as well as schematic structure figures prepared using Protein Data Bank (PDB) entries. ... the book is a pleasure to read." (Zygmunt Derewenda, Crystallography Reviews, May, 2016)

Spis treści

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

O autorze

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.