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

Scott, David J.

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.

Citation

Scott, D. J. (2016). Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins. Biophysical Reviews, 8(4), https://doi.org/10.1007/s12551-016-0235-5

• Journal Article Type: Article
• Acceptance Date: Oct 14, 2016
• Online Publication Date: Nov 22, 2016
• Publication Date: Dec 31, 2016
• Deposit Date: Apr 21, 2017
• Publicly Available Date: Apr 21, 2017
• Journal: Biophysical Reviews
• Print ISSN: 1867-2450
• Electronic ISSN: 1867-2450
• Publisher: Springer Verlag
• Peer Reviewed: Peer Reviewed
• Volume: 8
• Issue: 4
• DOI: https://doi.org/10.1007/s12551-016-0235-5
• Keywords: Small-angle scattering, Thermodynamic non-ideality, Guinier region
• Public URL: https://nottingham-repository.worktribe.com/output/831481
• Publisher URL: http://link.springer.com/article/10.1007%2Fs12551-016-0235-5