Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteinsTools 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 Full text not available from this repository.AbstractHydrodynamic 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.
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