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 Institute for Interdisciplinary Science

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 - 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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