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

Indirect allosteric effects of a neutral mutation: Structure of deoxyhaemoglobin North Chicago (ProC2(36)β → Ser)

Therapeutic agents for sickle cell disease.

The crystals are apparently orthorhombic; their unit-cell dimensions and the intensities of the 00l reflexions suggest a structure closely related to monoclinic methaemoglobin. Each structure appears to contain the same molecular layers parallel to (001), but in the monoclinic form the molecules are tilted the same way in each layer, while in the new form the tilt is alternately left and right in successive layers. Precession pictures show an interesting sequence of sharp and diffuse layer lines, those with certain indices h containing streaks parallel to c$^{\ast}$. In other layer lines the spots are broadened in varying degrees. The amplitudes of the h0l reflexions are related to the molecular Fourier transform described in previous papers of this series. Each value of F(h0l) is compounded from the sum or the difference of the amplitude at two points on the transform having the co-ordinates ha$^{\ast}$ 0 lc$^{\ast}$ and ha$^{\ast}$ 0 $\overline{l}$c$^{\ast}$. The rules for addition and subtraction of amplitudes follow a simple scheme which is related to the sequence of sharp and diffuse layers. The scheme accounts for all observed values of F(h0l), a reliability factor of 0$\cdot $21 being obtained. This correlation provides an independent check for the sequence of signs along certain layer lines of the transform. A preliminary analysis of the structure is made, and molecules in neighbouring layers are shown to be displaced by 11$\cdot $2 angstrom in the a direction.

Max F. Perutz

Papers

Indirect allosteric effects of a neutral mutation: Structure of deoxyhaemoglobin North Chicago (ProC2(36)β → Ser)

Therapeutic agents for sickle cell disease.

The structure of haemoglobin - V. Imidazole-methaemoglobin: a further check of the signs

Structure of hæmoglobin

Structure-function relationships in the low-affinity mutant haemoglobin aalborg (Gly74 (E18)β → Arg)