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2D: Protein Folding - in Vivo and in Vitro

  • Page ID
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    Learning Objectives

    • differentiate between thermodynamic (equilibrium) and kinetic (timed) approaches to the study of protein folding reactions
    • describe techniques to study transient (kinetic) and long-lived (thermodynamic) intermediates in protein folding
    • describe the following intermediates in protein folding: molten globule, X-Pro isomers; Disulfide bond intermediates
    • interpret spectral and chromatographic data from protein folding studies and use this to determine or explain a mechanism for folding
    • describe properties of folded, unfolded, molten globule, and intrinsically disordered proteins
    • explain the difference between the environments for protein folding when performed in vitro and in vivo
    • state the role of molecular chaperones in in vivo protein folding
    • describe differences in disulfide bond occurrence in cytoplasmic and extracellular proteins

    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 2D: Protein Folding - in Vivo and in Vitro is shared under a CC BY-NC-SA license and was authored, remixed, and/or curated by Henry Jakubowski.

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