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 | |
| Publication status | Published - Nov 1 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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Imamura, H., Morita, T., Sumi, T., Isogai, Y., Kato, M., & Nishikawa, K. (2013). Modulation of the intermolecular interaction of myoglobin by removal of the heme. Journal of Synchrotron Radiation, 20(6), 919-922. https://doi.org/10.1107/S0909049513022772