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Max F. Perutz

Bio: 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.
Topics: Hemoglobin, Bohr effect, Heme, Globin, Myoglobin


Papers
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Journal ArticleDOI
21 Nov 1970-Nature
TL;DR: The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect of oxygen itself.
Abstract: The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect of oxygen itself. The oxygen-free form is constrained by salt-bridges which are broken by the energy of haem–haem interaction with the release of H+. 2,3-Diphosphoglycerate may add to the constraints by being stereochemically complementary to a site between the β-chains ; this complementarity is lost on oxygenation.

2,625 citations

Journal ArticleDOI
TL;DR: Molecular modeling followed by optical, electron, and x-ray diffraction studies of a synthetic poly(L-glutamine) shows that it forms beta-sheets strongly held together by hydrogen bonds.
Abstract: Four inherited neurodegenerative diseases are linked to abnormally expanded repeats of glutamine residues in the affected proteins. Molecular modeling followed by optical, electron, and x-ray diffraction studies of a synthetic poly(L-glutamine) shows that it forms beta-sheets strongly held together by hydrogen bonds. Glutamine repeats may function as polar zippers, for example, by joining specific transcription factors bound to separate DNA segments. Their extension may cause disease either by increased, nonspecific affinity between such factors or by gradual precipitation of the affected proteins in neurons.

1,049 citations

Journal ArticleDOI
13 Jul 1968-Nature
TL;DR: The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.
Abstract: The secondary structure of the haemoglobin chains is similar to that of myoglobin, but some of the helical segments are more irregular and some parts of the non-helical segments have different conformations. The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.

847 citations

Journal ArticleDOI
TL;DR: It is of interest that the aromatic hydrogen bond arises from small partial charges centred on the ring carbon and hydrogen atoms: there is no need to consider delocalized electrons.

651 citations


Cited by
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Book ChapterDOI
01 Jan 1969

10,262 citations

Journal ArticleDOI
TL;DR: A new method, based on chemical thermodynamics, is developed for automatic detection of macromolecular assemblies in the Protein Data Bank (PDB) entries that are the results of X-ray diffraction experiments, as found, biological units may be recovered at 80-90% success rate, which makesX-ray crystallography an important source of experimental data on macromolescular complexes and protein-protein interactions.

8,377 citations

Journal ArticleDOI
TL;DR: "It is certain that all bodies whatsoever, though they have no sense, yet they have perception, and whether the body be alterant or alterec, evermore a perception precedeth operation; for else all bodies would be like one to another."

8,157 citations

Journal ArticleDOI
TL;DR: An analysis of the solvent content of 116 different crystal forms of globular proteins found that in many cases this range will be sufficiently restrictive to enable the probable number of molecules in the crystallographic asymmetric unit to be determined directly from the molecular weight of the protein and the space group and unit cell dimensions of the crystal.

7,857 citations

Journal ArticleDOI
20 Jul 1973-Science
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
Abstract: Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for \"their contribution to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule.\" In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the \"Thermodynamic Hypothesis,\" and outlined potential avenues of current and future scientific exploration.

6,520 citations