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Updated: May 7, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Modulation of the intermolecular interaction of myoglobin by removal of the heme
Hiroshi Imamura1, Takeshi Morita, Tomonari Sumi
1Graduate School of Advanced Integration Science, Chiba University, 1-33 Yayoi, Inage, Chiba 263-8522, Japan.
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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