Abstract
A small-angle X-ray scattering has been used to probe protein-protein interaction in solution. Conventional methods need to input modeled potentials with variable/invariable parameters to reproduce the experimental structure factor. In the present study, a model-free method for extracting the excess part of effective interaction potential between proteinmolecules in solutions over an introduced hard-sphere potential by using experimental data of small-angle X-ray scattering is presented on the basis of liquid-state integral equation theory. The reliability of the model-free method is tested by the application to experimentally derived structure factors for dense lysozyme solutions with different solution conditions [Javid et al., Phys. Rev. Lett. 99, 028101 (2007), Schroer et al., Phys. Rev. Lett. 106, 178102 (2011)]. The structure factors calculated from themodel-free method agree well with the experimental ones. The model-free method provides the following picture of the lysozyme solution: these are the stabilization of contact-pair configurations, large activation barrier against their formations, and screened Coulomb repulsion between the charged proteins. In addition, the model-free method will be useful to verify whether or not a model for colloidal system is acceptable to describing protein-protein interaction.
| Original language | English |
|---|---|
| Pages (from-to) | 42-46 |
| Number of pages | 5 |
| Journal | Journal of Molecular Liquids |
| Volume | 200 |
| Issue number | PA |
| DOIs | |
| Publication status | Published - 2014 |
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Keywords
- DLVO model
- Integral equation
- Liquid state theory
- Lysozyme
- Protein solutions
- Protein-protein interaction
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Spectroscopy
- Condensed Matter Physics
- Atomic and Molecular Physics, and Optics
- Electronic, Optical and Magnetic Materials
- Materials Chemistry
Cite this
A model-free method for extracting interaction potential between protein molecules using small-angle X-ray scattering. / Sumi, Tomonari; Imamura, Hiroshi; Morita, Takeshi; Nishikawa, Keiko.
In: Journal of Molecular Liquids, Vol. 200, No. PA, 2014, p. 42-46.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A model-free method for extracting interaction potential between protein molecules using small-angle X-ray scattering
AU - Sumi, Tomonari
AU - Imamura, Hiroshi
AU - Morita, Takeshi
AU - Nishikawa, Keiko
PY - 2014
Y1 - 2014
N2 - A small-angle X-ray scattering has been used to probe protein-protein interaction in solution. Conventional methods need to input modeled potentials with variable/invariable parameters to reproduce the experimental structure factor. In the present study, a model-free method for extracting the excess part of effective interaction potential between proteinmolecules in solutions over an introduced hard-sphere potential by using experimental data of small-angle X-ray scattering is presented on the basis of liquid-state integral equation theory. The reliability of the model-free method is tested by the application to experimentally derived structure factors for dense lysozyme solutions with different solution conditions [Javid et al., Phys. Rev. Lett. 99, 028101 (2007), Schroer et al., Phys. Rev. Lett. 106, 178102 (2011)]. The structure factors calculated from themodel-free method agree well with the experimental ones. The model-free method provides the following picture of the lysozyme solution: these are the stabilization of contact-pair configurations, large activation barrier against their formations, and screened Coulomb repulsion between the charged proteins. In addition, the model-free method will be useful to verify whether or not a model for colloidal system is acceptable to describing protein-protein interaction.
AB - A small-angle X-ray scattering has been used to probe protein-protein interaction in solution. Conventional methods need to input modeled potentials with variable/invariable parameters to reproduce the experimental structure factor. In the present study, a model-free method for extracting the excess part of effective interaction potential between proteinmolecules in solutions over an introduced hard-sphere potential by using experimental data of small-angle X-ray scattering is presented on the basis of liquid-state integral equation theory. The reliability of the model-free method is tested by the application to experimentally derived structure factors for dense lysozyme solutions with different solution conditions [Javid et al., Phys. Rev. Lett. 99, 028101 (2007), Schroer et al., Phys. Rev. Lett. 106, 178102 (2011)]. The structure factors calculated from themodel-free method agree well with the experimental ones. The model-free method provides the following picture of the lysozyme solution: these are the stabilization of contact-pair configurations, large activation barrier against their formations, and screened Coulomb repulsion between the charged proteins. In addition, the model-free method will be useful to verify whether or not a model for colloidal system is acceptable to describing protein-protein interaction.
KW - DLVO model
KW - Integral equation
KW - Liquid state theory
KW - Lysozyme
KW - Protein solutions
KW - Protein-protein interaction
UR - http://www.scopus.com/inward/record.url?scp=84949135644&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84949135644&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2014.03.014
DO - 10.1016/j.molliq.2014.03.014
M3 - Article
AN - SCOPUS:84949135644
VL - 200
SP - 42
EP - 46
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
SN - 0167-7322
IS - PA
ER -