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 journalArticle

5 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 languageEnglish
Pages (from-to)919-922
Number of pages4
JournalJournal of Synchrotron Radiation
Volume20
Issue number6
DOIs
Publication statusPublished - Nov 2013

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myoglobin
Modulation
proteins
Proteins
modulation
interactions
X ray scattering
Agglomeration
interference
Molecules
scattering
molecules
x rays

Keywords

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

ASJC Scopus subject areas

  • Instrumentation
  • Nuclear and High Energy Physics
  • Radiation

Cite this

Modulation of the intermolecular interaction of myoglobin by removal of the heme. / Imamura, Hiroshi; Morita, Takeshi; Sumi, Tomonari; Isogai, Yasuhiro; Kato, Minoru; Nishikawa, Keiko.

In: Journal of Synchrotron Radiation, Vol. 20, No. 6, 11.2013, p. 919-922.

Research output: Contribution to journalArticle

Imamura, Hiroshi ; Morita, Takeshi ; Sumi, Tomonari ; Isogai, Yasuhiro ; Kato, Minoru ; Nishikawa, Keiko. / Modulation of the intermolecular interaction of myoglobin by removal of the heme. In: Journal of Synchrotron Radiation. 2013 ; Vol. 20, No. 6. pp. 919-922.
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