Protein diffusion in crowded electrolyte solutions.
We report on a combined cold neutron backscattering and spin-echo study of the short-range and long-range nanosecond diffusion of the model globular protein bovine serum albumin (BSA) in aqueous solution as a function of protein concentration and NaCl salt concentration. Complementary small angle X-...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2010
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| _version_ | 1797097253098225664 |
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| author | Roosen-Runge, F Hennig, M Seydel, T Zhang, F Skoda, M Zorn, S Jacobs, R Maccarini, M Fouquet, P Schreiber, F |
| author_facet | Roosen-Runge, F Hennig, M Seydel, T Zhang, F Skoda, M Zorn, S Jacobs, R Maccarini, M Fouquet, P Schreiber, F |
| author_sort | Roosen-Runge, F |
| collection | OXFORD |
| description | We report on a combined cold neutron backscattering and spin-echo study of the short-range and long-range nanosecond diffusion of the model globular protein bovine serum albumin (BSA) in aqueous solution as a function of protein concentration and NaCl salt concentration. Complementary small angle X-ray scattering data are used to obtain information on the correlations of the proteins in solution. Particular emphasis is put on the effect of crowding, i.e. conditions under which the proteins cannot be considered as objects independent of each other. We thus address the question at which concentration this crowding starts to influence the static and in particular also the dynamical behaviour. We also briefly discuss qualitatively which charge effects, i.e. effects due to the interplay of charged molecules in an electrolyte solution, may be anticipated. Both the issue of crowding as well as that of charge effects are particularly relevant for proteins and their function under physiological conditions, where the protein volume fraction can be up to approximately 40% and salt ions are ubiquitous. The interpretation of the data is put in the context of existing studies on related systems and of existing theoretical models. |
| first_indexed | 2024-03-07T04:52:51Z |
| format | Journal article |
| id | oxford-uuid:d591aa70-e8d9-4c1d-8967-c5056440dcfc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:52:51Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:d591aa70-e8d9-4c1d-8967-c5056440dcfc2022-03-27T08:26:55ZProtein diffusion in crowded electrolyte solutions.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d591aa70-e8d9-4c1d-8967-c5056440dcfcEnglishSymplectic Elements at Oxford2010Roosen-Runge, FHennig, MSeydel, TZhang, FSkoda, MZorn, SJacobs, RMaccarini, MFouquet, PSchreiber, FWe report on a combined cold neutron backscattering and spin-echo study of the short-range and long-range nanosecond diffusion of the model globular protein bovine serum albumin (BSA) in aqueous solution as a function of protein concentration and NaCl salt concentration. Complementary small angle X-ray scattering data are used to obtain information on the correlations of the proteins in solution. Particular emphasis is put on the effect of crowding, i.e. conditions under which the proteins cannot be considered as objects independent of each other. We thus address the question at which concentration this crowding starts to influence the static and in particular also the dynamical behaviour. We also briefly discuss qualitatively which charge effects, i.e. effects due to the interplay of charged molecules in an electrolyte solution, may be anticipated. Both the issue of crowding as well as that of charge effects are particularly relevant for proteins and their function under physiological conditions, where the protein volume fraction can be up to approximately 40% and salt ions are ubiquitous. The interpretation of the data is put in the context of existing studies on related systems and of existing theoretical models. |
| spellingShingle | Roosen-Runge, F Hennig, M Seydel, T Zhang, F Skoda, M Zorn, S Jacobs, R Maccarini, M Fouquet, P Schreiber, F Protein diffusion in crowded electrolyte solutions. |
| title | Protein diffusion in crowded electrolyte solutions. |
| title_full | Protein diffusion in crowded electrolyte solutions. |
| title_fullStr | Protein diffusion in crowded electrolyte solutions. |
| title_full_unstemmed | Protein diffusion in crowded electrolyte solutions. |
| title_short | Protein diffusion in crowded electrolyte solutions. |
| title_sort | protein diffusion in crowded electrolyte solutions |
| work_keys_str_mv | AT roosenrungef proteindiffusionincrowdedelectrolytesolutions AT hennigm proteindiffusionincrowdedelectrolytesolutions AT seydelt proteindiffusionincrowdedelectrolytesolutions AT zhangf proteindiffusionincrowdedelectrolytesolutions AT skodam proteindiffusionincrowdedelectrolytesolutions AT zorns proteindiffusionincrowdedelectrolytesolutions AT jacobsr proteindiffusionincrowdedelectrolytesolutions AT maccarinim proteindiffusionincrowdedelectrolytesolutions AT fouquetp proteindiffusionincrowdedelectrolytesolutions AT schreiberf proteindiffusionincrowdedelectrolytesolutions |