Max Ferdinand Perutz OM CH CBE. 19 May 1914 – 6 February 2002

@article{Blow2004MaxFP,
  title={Max Ferdinand Perutz OM CH CBE. 19 May 1914 – 6 February 2002},
  author={David Blow},
  journal={Biographical Memoirs of Fellows of the Royal Society},
  year={2004},
  pages={227 - 256}
}
  • D. Blow
  • Published 1 December 2004
  • Physics
  • Biographical Memoirs of Fellows of the Royal Society
Scientists will remember Max Perutz for his outstanding analysis of the molecular structure, properties and allosteric mechanism of haemoglobin, but his wonderful clarity and simplicity in writing on the widest range of topics has made him famous far beyond the haemoglobin fraternity. He left many autobiographical essays on different events in his life, and his writings are quoted frequently in this memoir. Indeed, to a large extent, it is written by Max Perutz himself! 
1 Citations

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David Mervyn Blow. 27 June 1931 — 8 June 2004
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David Blow helped build the foundations of protein crystallography and transform it into a highly effective methodology and made fundamental contributions to the two principal methods of structure determination inprotein crystallography, known as isomorphous replacement and molecular replacement.

References

SHOWING 1-10 OF 25 REFERENCES
Protein Structure: New Approaches to Disease and Therapy
Dr Max Perutz, together with John Kendrew, received the 1962 Nobel Prize for Chemistry for using X-ray crystallography to solve the first two protein structures: haemoglobin and myoglobin. This paved
An X-Ray Study of Chymotrypsin and Hæmoglobin
We have recently been fortunate in obtaining well-developed crystals of two proteins—chymo-trypsin and haemoglobin. The former were prepared for us by Dr. Northrop of Princeton and the latter
A New View of Darwinism
I AM much obliged to Mr. Howorth for his courteous expressions towards me in the letter in your last number. If he will be so good as to look at p. 111 and p. 148, vol. ii. of my “Variation of
I wish I'd made you angry earlier
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
The 1.5-A. Reflexion from Proteins and Polypeptides
IN a recent issue of Nature, Pauling and Corey1 have raised certain points in connexion with the 1.5-A. reflexion which I reported to be present in proteins of the α-keratin type, in an artificial
Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model
TLDR
The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.
Molecular Pathology of Human Haemoglobin: Stereochemical Interpretation of Abnormal Oxygen Affinities
TLDR
The atomic model of oxyhaemoglobin showed that the haemoglobin molecule is insensitive to replacements of most amino-acid residues on its surface but extremely sensitive to quite small alterations of internal non-polar contacts.
The structure of haemoglobin III. Direct determination of the molecular transform
  • M. Perutz
  • Chemistry
    Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
  • 1954
Horse methaemoglobin crystallizes with two molecules in a face-centred monoclinic unit cell (space group C2), in which rigid layers of molecules parallel to (001) alternate with layers of liquid. The
Polar zipper sequence in the high-affinity hemoglobin of Ascaris suum: amino acid sequence and structural interpretation.
  • I. de Baere, L. Liu, M. Perutz
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1992
TLDR
It is proposed that the amino acid sequence of Ascaris hemoglobin fails to explain its high oxygen affinity and that this represents a polar zipper sequence and that the C-terminal extensions are joined in an eight-stranded beta barrel at the center of the molecule.
Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases.
TLDR
It is argued that the stability of all three fractions is due to the multiplicity of hydrogen bonds between extended strands of glutamine repeats in the oligomers or within a beta-hairpin formed by the single glutamine repeat of each monomer.
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