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


Dive into the research topics of 'Modulation of the intermolecular interaction of myoglobin by removal of the heme'. Together they form a unique fingerprint.

Cite this