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 journalArticlepeer-review

    6 Citations (Scopus)


    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
    Issue number6
    Publication statusPublished - Nov 2013


    • 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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