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4.8: H. Protein Aggregates and Disease

  • Page ID
    132657
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    Learning Objectives

    • describe experimental evidence to show that protein misfolding and aggregation depends on the amino acid sequence and the environment in which folding occurs.
    • describe conditions in vitro that may promote aggregation and how these might be minimized in vivo
    • describe alternative conformations of prion proteins and relate them to a energy topology landscape
    • explain how prion diseases may be transmitted in the absence of genetic material

    Thumbnail: Structure of human hemoglobin. The proteins α and β subunits are in red and blue, and the iron-containing heme groups in green. From PDB: 1GZX​. (GNU; Proteopedia Hemoglobin).


    This page titled 4.8: H. Protein Aggregates and Disease is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by Henry Jakubowski.

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