World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
92
Citations
39890
World Ranking
1842
National Ranking
102

Research.com Recognitions

  • 1970 - Member of the National Academy of Sciences
  • 1966 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1962 - Nobel Prize for their studies of the structures of globular proteins
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Max F. Perutz was affiliated with the University of Cambridge in the United Kingdom. Their scientific career included significant engagement with the study of globular proteins, a focus that culminated in notable recognition within the academic community.

The scientist received several honors throughout their career. These included being named a Member of the National Academy of Sciences in 1970 and a Fellow of the American Association for the Advancement of Science (AAAS) in 1966. Additionally, they were a Member of the European Molecular Biology Organization (EMBO).

Perutz was awarded the Nobel Prize in 1962 for their studies of the structures of globular proteins. This award is a significant marker of their contributions to biochemistry and molecular biology.

Best Publications

  • Stereochemistry of cooperative effects in haemoglobin.

    M. F. Perutz

  • Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis

    M. F. Perutz;M. G. Rossmann;Ann F. Cullis;Hilary Muirhead

  • Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases

    Max F. Perutz;Tony Johnson;Masashi Suzuki;John T. Finch

  • Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model

    M. F. Perutz;H. Muirhead;J. M. Cox;L. C. G. Goaman

  • The crystal structure of human deoxyhaemoglobin at 1.74 A resolution

    G. Fermi;M.F. Perutz;B. Shaanan;R. Fourme

  • Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence

    M.F. Perutz;J.C. Kendrew;H.C. Watson

  • Aromatic rings act as hydrogen bond acceptors

    Michael Levitt;Max F. Perutz

  • Molecular Pathology of Human Haemoglobin

    M F Perutz;H Lehmann

  • Amyloid fibers are water-filled nanotubes

    M. F. Perutz;J. T. Finch;J. Berriman;A. Lesk

  • THE STEREOCHEMICAL MECHANISM OF THE COOPERATIVE EFFECTS IN HEMOGLOBIN REVISITED

    M. F. Perutz;A. J. Wilkinson;M. Paoli;G. G. Dodson

  • Mechanisms of Cooperativity and Allosteric Regulation in Proteins

    Max F. Perutz

  • Stereochemistry of cooperative mechanisms in hemoglobin

    M.F. Perutz;G. Fermi;B. Luisi;B. Shaanan

  • Structure and function of haemoglobin

    M.F. Perutz

  • Glutamine repeats and neurodegenerative diseases: molecular aspects

    Max F Perutz

  • Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron.

    Unknown

  • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2.

    M F Perutz;H Raidt

  • Nature of Haem–Haem Interaction

    M. F. Perutz

  • The rhombotin family of cysteine-rich LIM-domain oncogenes: distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13.

    T Boehm;L Foroni;Y Kaneko;M F Perutz

  • STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION.

    Hilary Muirhead;M. F. Perutz

  • STRUCTURE AND MECHANISM OF HAEMOGLOBIN

    M. F. Perutz

  • New X-Ray Evidence on the Configuration of Polypeptide Chains: Polypeptide Chains in Poly-γ-benzyl- L -glutamate, Keratin and Hæmoglobin

    Perutz Mf

Frequent Co-Authors

Guy Dodson
Guy Dodson University of York
Angela M. Gronenborn
Angela M. Gronenborn University of Pittsburgh
Chien Ho
Chien Ho Carnegie Mellon University
Kiyoshi Nagai
Kiyoshi Nagai MRC Laboratory of Molecular Biology
Michael G. Rossmann
Michael G. Rossmann Purdue University West Lafayette
Terence H. Rabbitts
Terence H. Rabbitts Institute of Cancer Research
Ben F. Luisi
Ben F. Luisi University of Cambridge
Simon E. V. Phillips
Simon E. V. Phillips University of Oxford
Maurizio Brunori
Maurizio Brunori Sapienza University of Rome
Thomas Boehm
Thomas Boehm Max Planck Society

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Related Online Degrees & Career Pathways

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Best Scientists Citing Max F. Perutz