Pattern of cavities in globins: the case of human hemoglobin
Abstract In this paper we used the technique of filling with xenon atoms the hydrophobic cavities, previously referred to as packing defects, naturally present in myoglobin and hemoglobin. Our aim is to demonstrate up to which point the primary sequence is responsible for the globins’ function; and...
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ftzenodo:oai:zenodo.org:8116505 2023-07-30T04:07:06+02:00 Pattern of cavities in globins: the case of human hemoglobin savino carmelinda miele adriana draghi federica johnson kenneth sciara giuliano vallone beatrice maurizio brunori 2009-12-24 https://zenodo.org/record/8116505 https://doi.org/10.5281/zenodo.8116505 eng eng doi:10.5281/zenodo.8116504 https://zenodo.org/record/8116505 https://doi.org/10.5281/zenodo.8116505 oai:zenodo.org:8116505 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/legalcode Biopolymers 91(12) 1097-107 Globin fold Hydrophobic cavities Packing defects Structure-function relationship 3-CT-2004-506008X-ray diffraction info:eu-repo/semantics/article publication-article 2009 ftzenodo https://doi.org/10.5281/zenodo.811650510.5281/zenodo.8116504 2023-07-11T22:58:00Z Abstract In this paper we used the technique of filling with xenon atoms the hydrophobic cavities, previously referred to as packing defects, naturally present in myoglobin and hemoglobin. Our aim is to demonstrate up to which point the primary sequence is responsible for the globins’ function; and to shed light on the conservation of potential ligand docking sites and on their role in protein dynamics. In particular, we present the high resolution structures of Xe-adduct of wild type sperm whale myoglobin and for the first time those of wild type human hemoglobin and of a quadruple mutant (L(B10)Y and H(E7)Q in both α and β chains), both in deoxy form. The analysis revealed that the number and position of cavities is different in Mb and in α and β subunits, suggesting a different dynamics for ligand migration within the protein matrix. The number and position of hydrophobic cavities will be discussed also in view of the data available for other components of the globin superfamily. other grants acknowledged Italian MIUR FIRB2003 RBLA03B3KC_004. Article in Journal/Newspaper Sperm whale Zenodo |
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language |
English |
topic |
Globin fold Hydrophobic cavities Packing defects Structure-function relationship 3-CT-2004-506008X-ray diffraction |
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Globin fold Hydrophobic cavities Packing defects Structure-function relationship 3-CT-2004-506008X-ray diffraction savino carmelinda miele adriana draghi federica johnson kenneth sciara giuliano vallone beatrice maurizio brunori Pattern of cavities in globins: the case of human hemoglobin |
topic_facet |
Globin fold Hydrophobic cavities Packing defects Structure-function relationship 3-CT-2004-506008X-ray diffraction |
description |
Abstract In this paper we used the technique of filling with xenon atoms the hydrophobic cavities, previously referred to as packing defects, naturally present in myoglobin and hemoglobin. Our aim is to demonstrate up to which point the primary sequence is responsible for the globins’ function; and to shed light on the conservation of potential ligand docking sites and on their role in protein dynamics. In particular, we present the high resolution structures of Xe-adduct of wild type sperm whale myoglobin and for the first time those of wild type human hemoglobin and of a quadruple mutant (L(B10)Y and H(E7)Q in both α and β chains), both in deoxy form. The analysis revealed that the number and position of cavities is different in Mb and in α and β subunits, suggesting a different dynamics for ligand migration within the protein matrix. The number and position of hydrophobic cavities will be discussed also in view of the data available for other components of the globin superfamily. other grants acknowledged Italian MIUR FIRB2003 RBLA03B3KC_004. |
format |
Article in Journal/Newspaper |
author |
savino carmelinda miele adriana draghi federica johnson kenneth sciara giuliano vallone beatrice maurizio brunori |
author_facet |
savino carmelinda miele adriana draghi federica johnson kenneth sciara giuliano vallone beatrice maurizio brunori |
author_sort |
savino carmelinda |
title |
Pattern of cavities in globins: the case of human hemoglobin |
title_short |
Pattern of cavities in globins: the case of human hemoglobin |
title_full |
Pattern of cavities in globins: the case of human hemoglobin |
title_fullStr |
Pattern of cavities in globins: the case of human hemoglobin |
title_full_unstemmed |
Pattern of cavities in globins: the case of human hemoglobin |
title_sort |
pattern of cavities in globins: the case of human hemoglobin |
publishDate |
2009 |
url |
https://zenodo.org/record/8116505 https://doi.org/10.5281/zenodo.8116505 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biopolymers 91(12) 1097-107 |
op_relation |
doi:10.5281/zenodo.8116504 https://zenodo.org/record/8116505 https://doi.org/10.5281/zenodo.8116505 oai:zenodo.org:8116505 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/legalcode |
op_doi |
https://doi.org/10.5281/zenodo.811650510.5281/zenodo.8116504 |
_version_ |
1772820215505092608 |