Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography
Abstract The two hemoglobin structures determined by Max Perutz, the liganded R‐state, which has high oxygen affinity, and the unliganded T‐state with low oxygen affinity, were landmarks in molecular and structural biology (Perutz and Lehman, Nature 1968, 219, 902–909; Bolton and Perutz, Nature 1970...
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crwiley:10.1002/bip.21197 2024-06-02T07:58:14+00:00 Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography Dodson, Eleanor Dodson, Guy 2009 http://dx.doi.org/10.1002/bip.21197 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.21197 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.21197 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 91, issue 12, page 1056-1063 ISSN 0006-3525 1097-0282 journal-article 2009 crwiley https://doi.org/10.1002/bip.21197 2024-05-03T11:27:43Z Abstract The two hemoglobin structures determined by Max Perutz, the liganded R‐state, which has high oxygen affinity, and the unliganded T‐state with low oxygen affinity, were landmarks in molecular and structural biology (Perutz and Lehman, Nature 1968, 219, 902–909; Bolton and Perutz, Nature 1970, 28, 551–552; Perutz et al., Nature 1968, 219, 131–139). They provided the basis of a structural mechanism that connected beautifully to the theory of cooperativity in protein systems, formulated at about the same time by Monod et al. (J Mol Biol 1965, 12, 88–1118). Over the last 40 years there have been extensive biochemical and structural studies on hemoglobin's structure and the mechanisms that govern its co‐operativity, specificity, and other physiological properties. There are still however a number of unresolved issues over the molecule's properties, for example the mechanism responsible for the affects of pH on oxygen affinity, i.e., the Bohr and Root effects. In this communication the differences in the geometry at the a‐heme of unliganded and liganded human and the Antarctic fish ( Trematomus ) hemoglobin will be described and their relevance to affinity considered. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1056–1063, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic The Antarctic Bolton ENVELOPE(-62.967,-62.967,-65.017,-65.017) Perutz ENVELOPE(-66.367,-66.367,-67.617,-67.617) Biopolymers 91 12 1056 1063 |
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Wiley Online Library |
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English |
description |
Abstract The two hemoglobin structures determined by Max Perutz, the liganded R‐state, which has high oxygen affinity, and the unliganded T‐state with low oxygen affinity, were landmarks in molecular and structural biology (Perutz and Lehman, Nature 1968, 219, 902–909; Bolton and Perutz, Nature 1970, 28, 551–552; Perutz et al., Nature 1968, 219, 131–139). They provided the basis of a structural mechanism that connected beautifully to the theory of cooperativity in protein systems, formulated at about the same time by Monod et al. (J Mol Biol 1965, 12, 88–1118). Over the last 40 years there have been extensive biochemical and structural studies on hemoglobin's structure and the mechanisms that govern its co‐operativity, specificity, and other physiological properties. There are still however a number of unresolved issues over the molecule's properties, for example the mechanism responsible for the affects of pH on oxygen affinity, i.e., the Bohr and Root effects. In this communication the differences in the geometry at the a‐heme of unliganded and liganded human and the Antarctic fish ( Trematomus ) hemoglobin will be described and their relevance to affinity considered. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1056–1063, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com |
format |
Article in Journal/Newspaper |
author |
Dodson, Eleanor Dodson, Guy |
spellingShingle |
Dodson, Eleanor Dodson, Guy Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
author_facet |
Dodson, Eleanor Dodson, Guy |
author_sort |
Dodson, Eleanor |
title |
Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
title_short |
Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
title_full |
Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
title_fullStr |
Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
title_full_unstemmed |
Movements at the hemoglobin A‐hemes and their role in ligand binding, analyzed by X‐ray crystallography |
title_sort |
movements at the hemoglobin a‐hemes and their role in ligand binding, analyzed by x‐ray crystallography |
publisher |
Wiley |
publishDate |
2009 |
url |
http://dx.doi.org/10.1002/bip.21197 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.21197 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.21197 |
long_lat |
ENVELOPE(-62.967,-62.967,-65.017,-65.017) ENVELOPE(-66.367,-66.367,-67.617,-67.617) |
geographic |
Antarctic The Antarctic Bolton Perutz |
geographic_facet |
Antarctic The Antarctic Bolton Perutz |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biopolymers volume 91, issue 12, page 1056-1063 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.21197 |
container_title |
Biopolymers |
container_volume |
91 |
container_issue |
12 |
container_start_page |
1056 |
op_container_end_page |
1063 |
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1800741518171963392 |