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    Protein oligomerization in the bacterial outer membrane (Review)

    Meng, G.Y. and Chandran, Vidya and Remaut, Han and Fronzes, Remi and Waksman, Gabriel (2009) Protein oligomerization in the bacterial outer membrane (Review). Molecular Membrane Biology 26 (3), pp. 136-145. ISSN 0968-7688.

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    The formation of homo-oligomeric assemblies is a well-established characteristic of many soluble proteins and enzymes. Oligomerization has been shown to increase protein stability, allow allosteric cooperativity, shape reaction compartments and provide multivalent interaction sites in soluble proteins. In comparison, our understanding of the prevalence and reasons behind protein oligomerization in membrane proteins is relatively sparse. Recent progress in structural biology of bacterial outer membrane proteins has suggested that oligomerization may be as common and versatile as in soluble proteins. Here we review the current understanding of oligomerization in the bacterial outer membrane from a structural and functional point of view


    Item Type: Article
    Keyword(s) / Subject(s): Bacterial outer membrane, oligomerization, membrane protein, structural biology, β-barrel
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 04 Aug 2010 14:09
    Last Modified: 02 Aug 2023 16:49


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