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Fluorination in the Design of Membrane Protein Assemblies

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Membrane Proteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1063))

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Abstract

Protein design approaches based on the binary patterning of nonpolar and polar amino acids have been successful in generating native-like protein structures of amphiphilic α-helices or idealized amphiphilic β-strands in aqueous solution. Such patterning is not possible in the nonpolar environment of biological membranes, precluding the application of conventional approaches to the design of membrane proteins that assemble into discrete aggregates. This review surveys a promising, new strategy for membrane protein design that exploits the unique properties of fluorocarbons—in particular, their ability to phase separate from both water (due to their hydrophobicity) and hydrocarbons (due to their lipophobicity)—to generate membrane protein assemblies. The ability to design such discrete assemblies should enable the disruption of protein-protein interactions and provide templates for novel biomaterials and therapeutics.

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Author information

Authors and Affiliations

  1. Department of Chemistry, Tufts University, Medford, MA, USA

    Vijay M. Krishnamurthy & Krishna Kumar

  2. Cancer Center, Tufts Medical Center, Boston, MA, USA

    Krishna Kumar

Authors
  1. Vijay M. Krishnamurthy
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  2. Krishna Kumar
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Editor information

Editors and Affiliations

  1. Dept. of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, USA

    Giovanna Ghirlanda

  2. Department of Biochemistry, University of Wisconsin, Madison, Madison, Wisconsin, USA

    Alessandro Senes

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Krishnamurthy, V.M., Kumar, K. (2013). Fluorination in the Design of Membrane Protein Assemblies. In: Ghirlanda, G., Senes, A. (eds) Membrane Proteins. Methods in Molecular Biology, vol 1063. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-583-5_13

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  • DOI: https://doi.org/10.1007/978-1-62703-583-5_13

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-582-8

  • Online ISBN: 978-1-62703-583-5

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