Modulation of the intermolecular interaction of myoglobin by removal of the heme

Toward understanding intermolecular interactions governing self-association of proteins, the present study investigated a model protein, myoglobin, using a small-angle X-ray scattering technique. It has been known that removal of the heme makes myoglobin aggregation-prone. The interparticle interfer...

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Detalles Bibliográficos
Autores principales: Imamura, Hiroshi, Morita, Takeshi, Sumi, Tomonari, Isogai, Yasuhiro, Kato, Minoru, Nishikawa, Keiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Diffraction Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795556/
https://www.ncbi.nlm.nih.gov/pubmed/24121340
http://dx.doi.org/10.1107/S0909049513022772
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author Imamura, Hiroshi
Morita, Takeshi
Sumi, Tomonari
Isogai, Yasuhiro
Kato, Minoru
Nishikawa, Keiko
author_facet Imamura, Hiroshi
Morita, Takeshi
Sumi, Tomonari
Isogai, Yasuhiro
Kato, Minoru
Nishikawa, Keiko
author_sort Imamura, Hiroshi
collection PubMed
description Toward understanding intermolecular interactions governing self-association of proteins, the present study investigated a model protein, myoglobin, using a small-angle X-ray scattering technique. It has been known that removal of the heme makes myoglobin aggregation-prone. The interparticle interferences of the holomyoglobin and the apomyoglobin were compared in terms of the structure factor. Analysis of the structure factor using a model potential of Derjaguin–Laudau–Verwey–Overbeek (DLVO) suggests that the intermolecular interaction potential of apomyoglobin is more attractive than that of holomyoglobin at short range from the protein molecule.
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spelling pubmed-37955562013-10-15 Modulation of the intermolecular interaction of myoglobin by removal of the heme Imamura, Hiroshi Morita, Takeshi Sumi, Tomonari Isogai, Yasuhiro Kato, Minoru Nishikawa, Keiko J Synchrotron Radiat Diffraction Structural Biology Toward understanding intermolecular interactions governing self-association of proteins, the present study investigated a model protein, myoglobin, using a small-angle X-ray scattering technique. It has been known that removal of the heme makes myoglobin aggregation-prone. The interparticle interferences of the holomyoglobin and the apomyoglobin were compared in terms of the structure factor. Analysis of the structure factor using a model potential of Derjaguin–Laudau–Verwey–Overbeek (DLVO) suggests that the intermolecular interaction potential of apomyoglobin is more attractive than that of holomyoglobin at short range from the protein molecule. International Union of Crystallography 2013-11-01 2013-10-02 /pmc/articles/PMC3795556/ /pubmed/24121340 http://dx.doi.org/10.1107/S0909049513022772 Text en © Hiroshi Imamura et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Diffraction Structural Biology
Imamura, Hiroshi
Morita, Takeshi
Sumi, Tomonari
Isogai, Yasuhiro
Kato, Minoru
Nishikawa, Keiko
Modulation of the intermolecular interaction of myoglobin by removal of the heme
title Modulation of the intermolecular interaction of myoglobin by removal of the heme
title_full Modulation of the intermolecular interaction of myoglobin by removal of the heme
title_fullStr Modulation of the intermolecular interaction of myoglobin by removal of the heme
title_full_unstemmed Modulation of the intermolecular interaction of myoglobin by removal of the heme
title_short Modulation of the intermolecular interaction of myoglobin by removal of the heme
title_sort modulation of the intermolecular interaction of myoglobin by removal of the heme
topic Diffraction Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795556/
https://www.ncbi.nlm.nih.gov/pubmed/24121340
http://dx.doi.org/10.1107/S0909049513022772
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