Equilibrium clusters in concentrated lysozyme protein solutions
We have studied the structure of salt-free lysozyme at 293 K and pH 7.8 using molecular simulations and experimental SAXS effective potentials between proteins at three volume fractions, φ = 0.012, 0.033, and 0.12. We found that the structure of lysozyme near physiological conditions strongly depend...
| Main Authors: | , , , |
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| Format: | Journal Article |
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Elsevier
2011
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| Online Access: | http://hdl.handle.net/20.500.11937/35402 |
| _version_ | 1848754487507812352 |
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| author | Kowalczyk, Piotr Ciach, A. Gauden, P. Terzyk, A. |
| author_facet | Kowalczyk, Piotr Ciach, A. Gauden, P. Terzyk, A. |
| author_sort | Kowalczyk, Piotr |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | We have studied the structure of salt-free lysozyme at 293 K and pH 7.8 using molecular simulations and experimental SAXS effective potentials between proteins at three volume fractions, φ = 0.012, 0.033, and 0.12. We found that the structure of lysozyme near physiological conditions strongly depends on the volume fraction of proteins. The studied lysozyme solutions are dominated by monomers only for φ <= 0:012; for the strong dilution 70% of proteins are in a form of monomers. For φ = 0.033 only 20% of proteins do not belong to a cluster. The clusters are mainly elongated. For φ = 0.12 almost no individual particles exits, and branched, irregular clusters of large extent appear. Our simulation study provides new insight into the formation of equilibrium clusters in charged protein solutions near physiological conditions. |
| first_indexed | 2025-11-14T08:41:12Z |
| format | Journal Article |
| id | curtin-20.500.11937-35402 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T08:41:12Z |
| publishDate | 2011 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-354022018-03-29T09:08:49Z Equilibrium clusters in concentrated lysozyme protein solutions Kowalczyk, Piotr Ciach, A. Gauden, P. Terzyk, A. Scattering experiments Equilibrium clusters Salt-free lysozyme solutions Short-range attraction and weak long-range repulsion effective potential We have studied the structure of salt-free lysozyme at 293 K and pH 7.8 using molecular simulations and experimental SAXS effective potentials between proteins at three volume fractions, φ = 0.012, 0.033, and 0.12. We found that the structure of lysozyme near physiological conditions strongly depends on the volume fraction of proteins. The studied lysozyme solutions are dominated by monomers only for φ <= 0:012; for the strong dilution 70% of proteins are in a form of monomers. For φ = 0.033 only 20% of proteins do not belong to a cluster. The clusters are mainly elongated. For φ = 0.12 almost no individual particles exits, and branched, irregular clusters of large extent appear. Our simulation study provides new insight into the formation of equilibrium clusters in charged protein solutions near physiological conditions. 2011 Journal Article http://hdl.handle.net/20.500.11937/35402 10.1016/j.jcis.2011.07.043 Elsevier restricted |
| spellingShingle | Scattering experiments Equilibrium clusters Salt-free lysozyme solutions Short-range attraction and weak long-range repulsion effective potential Kowalczyk, Piotr Ciach, A. Gauden, P. Terzyk, A. Equilibrium clusters in concentrated lysozyme protein solutions |
| title | Equilibrium clusters in concentrated lysozyme protein solutions |
| title_full | Equilibrium clusters in concentrated lysozyme protein solutions |
| title_fullStr | Equilibrium clusters in concentrated lysozyme protein solutions |
| title_full_unstemmed | Equilibrium clusters in concentrated lysozyme protein solutions |
| title_short | Equilibrium clusters in concentrated lysozyme protein solutions |
| title_sort | equilibrium clusters in concentrated lysozyme protein solutions |
| topic | Scattering experiments Equilibrium clusters Salt-free lysozyme solutions Short-range attraction and weak long-range repulsion effective potential |
| url | http://hdl.handle.net/20.500.11937/35402 |