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  2. Chaperones are proteins that guide proteins along the proper pathways for folding. They protect proteins when they are in the process of folding, shielding them from other proteins that might bind and hinder the process.
    Chaperones prevent aggregation and incorrect folding by binding to and stabilizing partially or totally unfolded protein polypeptides until the polypeptide chain is fully synthesized. They also ensure the stability of unfolded polypeptide chains as they are transported into the subcellular organelles.
    info.gbiosciences.com/blog/how-chaperone-assiste…
    How do they work? Small-molecule chaperones act like molecular glue, holding various parts of the protein structure together through the favorable interactions (electrostatic, van der Waals, and hydrogen bonding) they make with residues in the binding site.
    jbiol.biomedcentral.com/articles/10.1186/jbiol186
     
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