Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins

Scott, David J. (2016) Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins. Biophysical Reviews, 8 (4). pp. 441-444. ISSN 1867-2450

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Abstract

Hydrodynamic studies of the solution properties of proteins and other biological macromolecules are often hard to interpret when the sample is present at a reasonably concentrated solution. The reason for this is that solutions exhibit deviations from ideal behaviour which is manifested as thermodynamic non-ideality. The range of concentrations at which this behaviour typically is exhibited is as low as 1-2 mg/ml, well within the range of concentrations used for their analysis by techniques such as small-angle scattering. Here we discuss thermodynamic non-ideality used previously used in the context of light scattering and sedimentation equilibrium analytical ultracentrifugation and apply it to the Guinier region of small-angle scattering data. The results show that there is a complementarity between the radially averaged structure factor derived from small-angle X-ray scattering/small-angle neutron scattering studies and the second virial coefficient derived from sedimentation equilibrium analytical ultracentrifugation experiments.

Item Type: Article
Keywords: Small-angle scattering, Thermodynamic non-ideality, Guinier region
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Biosciences
Identification Number: https://doi.org/10.1007/s12551-016-0235-5
Depositing User: Scott, David
Date Deposited: 21 Apr 2017 13:22
Last Modified: 04 Jun 2018 10:56
URI: http://eprints.nottingham.ac.uk/id/eprint/41954

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