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    Equilibrium clusters in concentrated lysozyme protein solutions

    Access Status
    Fulltext not available
    Authors
    Kowalczyk, Piotr
    Ciach, A.
    Gauden, P.
    Terzyk, A.
    Date
    2011
    Type
    Journal Article
    
    Metadata
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    Citation
    Kowalczyk, P. and Ciach, A. and Gauden, P.A. and Terzyk, A.P. 2011. Equilibrium clusters in concentrated lysozyme protein solutions. Journal of Colloid and Interface Science. 363 (2): pp. 579-584.
    Source Title
    Journal of Colloid and Interface Science
    DOI
    10.1016/j.jcis.2011.07.043
    ISSN
    00219797
    School
    Department of Applied Chemistry
    URI
    http://hdl.handle.net/20.500.11937/35402
    Collection
    • Curtin Research Publications
    Abstract

    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.

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