M
Max F. Perutz
Researcher at Laboratory of Molecular Biology
Publications - 198
Citations - 24791
Max F. Perutz is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Hemoglobin & Bohr effect. The author has an hindex of 74, co-authored 198 publications receiving 24297 citations. Previous affiliations of Max F. Perutz include Russian Academy of Sciences & University of York.
Papers
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Journal ArticleDOI
The Structure of Haemoglobin. II
TL;DR: The outer form of the haemoglobin molecule is delimited by considering the way in which it packs into a number of crystalline forms as discussed by the authors, and the evidence of form birefringence is compatible with these conclusions.
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Stereochemistry of iron in deoxyhaemoglobin.
TL;DR: Compared the EXAFS of deoxyhaemoglobin with that of the ferrous ‘picket fence’ 2-methylimidazole complex in which the displacement of the iron from the plane of the porphyrin nitrogens is known to be 0.399±0.004 and 0.426± 0.004 Å, consistent with similar displacements of the irons.
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The structure of haemoglobin. IX. A three-dimensional Fourier synthesis at 5.5 Å resolution: description of the structure
TL;DR: The electron density distribution in the unit cell is calculated at intervals of approximately 2Å and plotted in a series of sections parallel to (010) and shows that haemoglobin consists of four subunits in a tetrahedral array.
Book
Protein Structure: New Approaches to Disease and Therapy
TL;DR: In this article, the authors explored how the structure of biological macromolecules is determined, and how X-ray crystallographic studies have led to new insights into disease processes and opened new approaches to medical treatment.
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Physiological and x-ray studies of potential antisickling agents.
TL;DR: X-ray analysis showed that three pairs of molecules of cl ofibric acid, the active metabolite of clofibrate, bound to the walls of the internal cavity of deoxyhemoglobin A; only one pair bound to a quite different site, between helices A, E, and H of the alpha chains of carbon monoxide hemoglobin A.