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 2013 |
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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 journal › Article
}
TY - JOUR
T1 - Modulation of the intermolecular interaction of myoglobin by removal of the heme
AU - Imamura, Hiroshi
AU - Morita, Takeshi
AU - Sumi, Tomonari
AU - Isogai, Yasuhiro
AU - Kato, Minoru
AU - Nishikawa, Keiko
PY - 2013/11
Y1 - 2013/11
N2 - 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.
AB - 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.
KW - protein engineering
KW - protein-protein interaction
KW - small-angle X-ray scattering
UR - http://www.scopus.com/inward/record.url?scp=84885622275&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84885622275&partnerID=8YFLogxK
U2 - 10.1107/S0909049513022772
DO - 10.1107/S0909049513022772
M3 - Article
C2 - 24121340
AN - SCOPUS:84885622275
VL - 20
SP - 919
EP - 922
JO - Journal of Synchrotron Radiation
JF - Journal of Synchrotron Radiation
SN - 0909-0495
IS - 6
ER -