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

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 thermodyn...

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Main Author: Scott, David J.
Format: Article
Published: Springer Verlag 2016
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Online Access:https://eprints.nottingham.ac.uk/41954/
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author Scott, David J.
author_facet Scott, David J.
author_sort Scott, David J.
building Nottingham Research Data Repository
collection Online Access
description 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.
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spelling nottingham-419542020-05-04T18:23:45Z https://eprints.nottingham.ac.uk/41954/ Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins Scott, David J. 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. Springer Verlag 2016-12-31 Article PeerReviewed 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 Small-angle scattering Thermodynamic non-ideality Guinier region http://link.springer.com/article/10.1007%2Fs12551-016-0235-5 doi:10.1007/s12551-016-0235-5 doi:10.1007/s12551-016-0235-5
spellingShingle Small-angle scattering
Thermodynamic non-ideality
Guinier region
Scott, David J.
Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title_full Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title_fullStr Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title_full_unstemmed Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title_short Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins
title_sort accounting for thermodynamic non-ideality in the guinier region of small-angle scattering data of proteins
topic Small-angle scattering
Thermodynamic non-ideality
Guinier region
url https://eprints.nottingham.ac.uk/41954/
https://eprints.nottingham.ac.uk/41954/
https://eprints.nottingham.ac.uk/41954/