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

Hiroshi Imamura; Takeshi Morita; Tomonari Sumi; Yasuhiro Isogai; Minoru Kato; Keiko Nishikawa

doi:10.1107/S0909049513022772

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

Hiroshi Imamura, Takeshi Morita, Tomonari Sumi, Yasuhiro Isogai, Minoru Kato, Keiko Nishikawa

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	919-922
Number of pages	4
Journal	Journal of Synchrotron Radiation
Volume	20
Issue number	6
DOIs	https://doi.org/10.1107/S0909049513022772
Publication status	Published - Nov 2013

Keywords

protein engineering
protein-protein interaction
small-angle X-ray scattering

ASJC Scopus subject areas

Radiation
Nuclear and High Energy Physics
Instrumentation

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10.1107/S0909049513022772

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abstract = "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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T1 - Modulation of the intermolecular interaction of myoglobin by removal of the heme

AU - Imamura, Hiroshi

AU - Morita, Takeshi

AU - Sumi, Tomonari

AU - Isogai, Yasuhiro

AU - Kato, Minoru

AU - Nishikawa, Keiko

PY - 2013/11

Y1 - 2013/11

N2 - 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.

AB - 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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KW - protein-protein interaction

KW - small-angle X-ray scattering

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

Abstract

Keywords

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