The Discreet Charm of Protein Binding Sites

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.

"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)