A model-free method for extracting interaction potential between protein molecules using small-angle X-ray scattering

Tomonari Sumi, Hiroshi Imamura, Takeshi Morita, Keiko Nishikawa

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)42-46
Number of pages5
JournalJournal of Molecular Liquids
Volume200
Issue numberPA
DOIs
Publication statusPublished - 2014

Fingerprint

X ray scattering
proteins
Proteins
Molecules
scattering
lysozyme
molecules
Muramidase
x rays
interactions
Enzymes
Contacts (fluid mechanics)
Integral equations
integral equations
Stabilization
stabilization
Chemical activation
activation
probes
Liquids

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 journalArticle

@article{83e5d7d363064ef1b7c5c2c4548c9097,
title = "A model-free method for extracting interaction potential between protein molecules using small-angle X-ray scattering",
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.",
keywords = "DLVO model, Integral equation, Liquid state theory, Lysozyme, Protein solutions, Protein-protein interaction",
author = "Tomonari Sumi and Hiroshi Imamura and Takeshi Morita and Keiko Nishikawa",
year = "2014",
doi = "10.1016/j.molliq.2014.03.014",
language = "English",
volume = "200",
pages = "42--46",
journal = "Journal of Molecular Liquids",
issn = "0167-7322",
publisher = "Elsevier",
number = "PA",

}

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 -