Dynamics of highly concentrated protein solutions around the denaturing transition
Using both quasi-elastic and fixed-window neutron spectroscopy, we study the dynamics of highly concentrated aqueous protein solutions of bovine serum albumin around the denaturing transition. For the temperature range 280 K < T < 370 K, the total mean-squared displacement 〈u...
| Egile Nagusiak: | , , , , , , , |
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| Formatua: | Journal article |
| Hizkuntza: | English |
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2012
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| _version_ | 1826305987242360832 |
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| author | Hennig, M Roosen-Runge, F Zhang, F Zorn, S Skoda, M Jacobs, R Seydel, T Schreiber, F |
| author_facet | Hennig, M Roosen-Runge, F Zhang, F Zorn, S Skoda, M Jacobs, R Seydel, T Schreiber, F |
| author_sort | Hennig, M |
| collection | OXFORD |
| description | Using both quasi-elastic and fixed-window neutron spectroscopy, we study the dynamics of highly concentrated aqueous protein solutions of bovine serum albumin around the denaturing transition. For the temperature range 280 K < T < 370 K, the total mean-squared displacement 〈u 2〉 is recorded. Below and above the denaturing, we observe that 〈u 2〉 increases monotonically with T, but at the denaturing transition it decreases strongly. This observation can be rationalized and quantitatively modeled as a transition from a liquid protein solution to a gel-like state. Atomic vibrations, molecular subunit diffusion and, most importantly, diffusion of the entire protein determine 〈u 2〉. The latter is strongly hindered due to entanglement and cross-linking of the chains and causes the pronounced decrease of 〈u 2〉. Using information from the full quasi-elastic signal, we separate the diffusion contribution from 〈u 2〉 and reveal the transition temperature. For the analysis of this separation, we introduce a general concept, which is applicable to other colloid systems exhibiting both center-of-mass and internal dynamics. © 2012 The Royal Society of Chemistry. |
| first_indexed | 2024-03-07T06:41:06Z |
| format | Journal article |
| id | oxford-uuid:f94e9a9c-7cae-49b8-ac54-1d54838d2d20 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:41:06Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:f94e9a9c-7cae-49b8-ac54-1d54838d2d202022-03-27T12:57:06ZDynamics of highly concentrated protein solutions around the denaturing transitionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f94e9a9c-7cae-49b8-ac54-1d54838d2d20EnglishSymplectic Elements at Oxford2012Hennig, MRoosen-Runge, FZhang, FZorn, SSkoda, MJacobs, RSeydel, TSchreiber, FUsing both quasi-elastic and fixed-window neutron spectroscopy, we study the dynamics of highly concentrated aqueous protein solutions of bovine serum albumin around the denaturing transition. For the temperature range 280 K < T < 370 K, the total mean-squared displacement 〈u 2〉 is recorded. Below and above the denaturing, we observe that 〈u 2〉 increases monotonically with T, but at the denaturing transition it decreases strongly. This observation can be rationalized and quantitatively modeled as a transition from a liquid protein solution to a gel-like state. Atomic vibrations, molecular subunit diffusion and, most importantly, diffusion of the entire protein determine 〈u 2〉. The latter is strongly hindered due to entanglement and cross-linking of the chains and causes the pronounced decrease of 〈u 2〉. Using information from the full quasi-elastic signal, we separate the diffusion contribution from 〈u 2〉 and reveal the transition temperature. For the analysis of this separation, we introduce a general concept, which is applicable to other colloid systems exhibiting both center-of-mass and internal dynamics. © 2012 The Royal Society of Chemistry. |
| spellingShingle | Hennig, M Roosen-Runge, F Zhang, F Zorn, S Skoda, M Jacobs, R Seydel, T Schreiber, F Dynamics of highly concentrated protein solutions around the denaturing transition |
| title | Dynamics of highly concentrated protein solutions around the denaturing transition |
| title_full | Dynamics of highly concentrated protein solutions around the denaturing transition |
| title_fullStr | Dynamics of highly concentrated protein solutions around the denaturing transition |
| title_full_unstemmed | Dynamics of highly concentrated protein solutions around the denaturing transition |
| title_short | Dynamics of highly concentrated protein solutions around the denaturing transition |
| title_sort | dynamics of highly concentrated protein solutions around the denaturing transition |
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