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Table of contents

  1. Front Matter
    Pages i-xiii
    PDF
  2. Introduction
    Joseph Yariv
    Pages 1-17
    PDF
  3. Tubulin
    Joseph Yariv
    Pages 19-26
    PDF
  4. A Variety of Saccharide Binding-Sites
    Joseph Yariv
    Pages 27-37
    PDF
  5. The Secret of Protein Sophistication
    Joseph Yariv
    Pages 39-46
    PDF
  6. Curiouser Binding-Sites – In Membrane Transport Proteins
    Joseph Yariv
    Pages 47-57
    PDF
  7. Back Matter
    Pages 59-60
    PDF

About this book

Introduction

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.

Keywords

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 Structure by X-ray Crystallography

Authors and affiliations

  1. 1.CaesareaIsrael

About the authors

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.  

Bibliographic information

Reviews

“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)