CHAPTER 24 – Evolution of Protein Molecules

Inference of macromolecular assemblies from crystalline state.

On the Nature of Allosteric Transitions: A Plausible Model

Solvent content of protein crystals.

Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for \"their contribution\n to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease\n molecule.\" In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation\n for his work on protein folding and the \"Thermodynamic Hypothesis,\" and outlined potential avenues of current and\n future scientific exploration.

https://web.iitd.ac.in/~amittal/1973_Anfinsen_Science.pdf

Principles that Govern the Folding of Protein Chains

IT has been shown that very detailed X-ray diffraction photographs can be obtained from crystals of horse methaemoglobin suspended in concentrated solutions of ammonium sulphate. On rapid drying in air, these crystals contract by 42 per cent of their wet volume. The dried crystals give a poor diffraction pattern consisting of few low-order reflexions around the central spot1.

X-ray analysis of hæmoglobin

Relation between structure and sequence of haemoglobin.

Structure of human fluoromethaemoglobin with inositol hexaphosphate.

This delightful collection of essays by Nobel Laureate Max Perutz explores a wide range of scientific and personal topics with great insight and lucidity. The pages of the book are filled with stories of some of the intellectual giants of twentieth century science -- Pauling, Meitner, Medawar, Krebs and Jacob, among others. This book is intended for general reader with an interest in science and scientific personalities of the twentieth century.

I wish I'd made you angry earlier : essays on science, scientists, and humanity

The theory that the αβ dimer is the functional unit of cooperativity in hemoglobin has been tested by determination of the oxygen equilibrium curve of stable deoxy dimers, obtained by the addition of 0.9 M MgCl2 to human des-Arg 141α-hemoglobin. Cooperativity was absent in this medium, but was regained on transfer of the hemoglobin to a dilute phosphate buffer, where tetramers reformed. X-ray analysis of crystals of oxy- and deoxy-des-Arg hemoglobins showed that the removal of Arg 141α would leave the structure of αβ dimers unchanged. Nonreactivity of the sulfhydryl groups at 112β proved that the subunits in deoxy dimers form the same contact as in oxy dimers, namely α1β1, and that no significant dissociation into free subunits occurs in 0.9 M MgCl2. The absorption spectrum of the deoxy dimers corresponded to the sum of the spectra of the free deoxy α and β subunits, and was different from that of the deoxy tetramer, showing the constraining salt bridges formed by the C-terminal residues in the tetramer to be necessary for the spectral changes normally observed on association of the deoxy subunits.

Max F. Perutz

Papers

X-ray analysis of hæmoglobin

Relation between structure and sequence of haemoglobin.

Structure of human fluoromethaemoglobin with inositol hexaphosphate.

I wish I'd made you angry earlier : essays on science, scientists, and humanity

Noncooperativity of the αβ Dimer in the Reaction of Hemoglobin with Oxygen