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    The self assembly of proteins; probing patchy protein interactions


    James, Susan and Quinn, Michelle K. and McManus, Jennifer (2015) The self assembly of proteins; probing patchy protein interactions. Physical Chemistry Chemical Physics, 17 (7). pp. 5413-5420. ISSN 1463-9076

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    Abstract

    The ability to control the self-assembly of biological molecules to form defined structures, with a high degree of predictability is a central aim for soft matter science and synthetic biology. Several examples of this are known for synthetic systems, such as anisotropic colloids. However, for biomacromolecules, such as proteins, success has been more limited, since aeolotopic (or anisotropic) interactions between protein molecules are not easily predicted. We have created three double mutants of human gD-crystallin for which the phase diagrams for singly mutated proteins can be used to predict the behavior of the double mutants. These proteins provide a robust mechanism to examine the kinetic and thermodynamic properties of proteins in which competing interactions exist due to the anisotropic or patchy nature of the protein surface.

    Item Type: Article
    Additional Information: The definitive version of this article is available at DOI: 10.1039/c4cp05892e . This work was made possible by Science Foundation Grant 11/RFP.1/PHY/3165, the Irish Research Council and SFI Stokes Lectureship to JJMcM. The authors thank Nicolette Lubsen for permission to use the HGD plasmid DNA
    Keywords: self assembly; proteins; protein interactions;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Item ID: 6027
    Identification Number: https://doi.org/10.1039/c4cp05892e
    Depositing User: Jennifer McManus
    Date Deposited: 14 Apr 2015 15:27
    Journal or Publication Title: Physical Chemistry Chemical Physics
    Publisher: Royal Society of Chemistry
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI), Irish Research Council for Science Engineering and Technology (IRCSET)
    URI:

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