J_MoleculLiq_200_42.pdf 1.28 MB
Sumi, Tomonari Department of Chemistry, Faculty of Science, Okayama University ORCID Kaken ID publons researchmap
Imamura, Hiroshi Graduate School of Advanced integration Science, Chiba University
Morita, Takeshi Graduate School of Advanced integration Science, Chiba University
Nishikawa, Keiko Graduate School of Advanced integration Science, Chiba University
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 protein molecules 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 the model-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.
Liquid state theory
Journal of Molecular Liquids
|Web of Science KeyUT|
Tomonari Sumi, Hiroshi Imamura, Takeshi Morita, Keiko Nishikawa, A model-free method for extracting interaction potential between protein molecules using small-angle X-ray scattering, Journal of Molecular Liquids, Volume 200, Part A, 2014, Pages 42-46, ISSN 0167-7322, https://doi.org/10.1016/j.molliq.2014.03.014.
Ministry of Education, Culture, Sports, Science and Technology
25610121 : Chemomechanical network modeling for molecular motor dynamics of kinesin