Low- <i>Q</i> Asymptotic Behavior of the Effective Structure Factor Yields Model-Independent Radius of Interparticle Interaction ( <i>R</i> <sub> <i>i</i> </sub> )

Guinier analysis has been extensively used in academic and industrial research settings to obtain the model-independent size of a polymer, protein, or colloid in solution from small-angle scattering data. Using the Guinier model, the radius of gyration (<i>R</i> <sub><i>g</i></sub> ) is extracted from the form factor at low <i>Q</i>. Here, we develop an analogous approach for analyzing the effective structure factor data at low <i>Q</i> to extract a model-independent radius of interaction potential, <i>R</i> <sub><i>i</i></sub> . Whereas <i>R</i> <sub><i>g</i></sub> describes how spread out the scattering length density distribution of particles is from their center of mass, <i>R</i> <sub><i>i</i></sub> is an effective root-mean-square distance that quantifies how far the interparticle correlation deviates from its ideal gas configuration due to interactions. We demonstrate this novel analysis method by applying it to experimental small-angle neutron scattering data on lysozyme protein solutions. We discuss its broad implications for analysis of low-<i>Q</i> asymptotic X-ray and neutron scattering data, where Guinier analysis is traditionally applied.

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Journal
ACS Measurement Science Au
Published
2025-11-07
DOI
https://doi.org/10.1021/acsmeasuresciau.5c00099
Primary Topic
Enzyme Structure and Function
Type
article
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article

Low- Q Asymptotic Behavior of the Effective Structure Factor Yields Model-Independent Radius of Interparticle Interaction ( R i )

Wellington Leite, Chelsea E. R. Edwards, Yun Liu
ACS Measurement Science Au
Enzyme Structure and Function
article

Low- Q Asymptotic Behavior of the Effective Structure Factor Yields Model-Independent Radius of Interparticle Interaction ( R i )

Wellington Leite, Chelsea E. R. Edwards, Yun Liu
article en

Abstract

Guinier analysis has been extensively used in academic and industrial research settings to obtain the model-independent size of a polymer, protein, or colloid in solution from small-angle scattering data. Using the Guinier model, the radius of gyration (<i>R</i> <sub><i>g</i></sub> ) is extracted from the form factor at low <i>Q</i>. Here, we develop an analogous approach for analyzing the effective structure factor data at low <i>Q</i> to extract a model-independent radius of interaction potential, <i>R</i> <sub><i>i</i></sub> . Whereas <i>R</i> <sub><i>g</i></sub> describes how spread out the scattering length density distribution of particles is from their center of mass, <i>R</i> <sub><i>i</i></sub> is an effective root-mean-square distance that quantifies how far the interparticle correlation deviates from its ideal gas configuration due to interactions. We demonstrate this novel analysis method by applying it to experimental small-angle neutron scattering data on lysozyme protein solutions. We discuss its broad implications for analysis of low-<i>Q</i> asymptotic X-ray and neutron scattering data, where Guinier analysis is traditionally applied.

ACS Measurement Science AuVol. 6(1)
Oak Ridge National Laboratory (US), National Institute of Standards and Technology (US), National Institute of Standards (EG), NIST Center for Neutron Research (US), University of Delaware (US)
Openalex Percentile: Top 74%
Enzyme Structure and Function
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Low- <i>Q</i> Asymptotic Behavior of the Effective Structure Factor Yields Model-Independent Radius of Interparticle Interaction ( <i>R</i> <sub> <i>i</i> </sub> ) — Wellington Leite, Chelsea E. R. Edwards, et al. · ACS Measurement Science Au (2025) | TGRS Research Map | TGRS