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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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Autor principal: Scott, David J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5283502/
https://www.ncbi.nlm.nih.gov/pubmed/28203306
http://dx.doi.org/10.1007/s12551-016-0235-5
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author Scott, David J.
author_facet Scott, David J.
author_sort Scott, David J.
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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 pubmed-52835022017-02-13 Accounting for thermodynamic non-ideality in the Guinier region of small-angle scattering data of proteins Scott, David J. Biophys Rev Brief Communication 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 Berlin Heidelberg 2016-11-22 /pmc/articles/PMC5283502/ /pubmed/28203306 http://dx.doi.org/10.1007/s12551-016-0235-5 Text en © The Author(s) 2016 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, duplication, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Brief Communication
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 Brief Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5283502/
https://www.ncbi.nlm.nih.gov/pubmed/28203306
http://dx.doi.org/10.1007/s12551-016-0235-5
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