Do Chaperonins Boost Protein Yields by Accelerating Folding or Preventing Aggregation?
نویسندگان
چکیده
منابع مشابه
Translocation boost protein-folding efficiency of double-barreled chaperonins.
Incorrect folding of proteins in living cells may lead to malfunctioning of the cell machinery. To prevent such cellular disasters from happening, all cells contain molecular chaperones that assist nonnative proteins in folding into the correct native structure. One of the most studied chaperone complexes is the GroEL-GroES complex. The GroEL part has a "double-barrel" structure, which consists...
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The Escherichia coli chaperone GroEL epitomizes the group of chaperone proteins termed as chaperonins. The wealth of structural and functional information available for GroEL, and its accessory protein, the co-chaperonin GroES, has been of much value in deciphering the role of chaperonins in facilitating the folding of substrate proteins in the cell. The chaperonin machinery has a complex archi...
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Protein folding is a biological process that is essential for the proper functioning of proteins in all living organisms. In cells, many proteins require the assistance of molecular chaperones for their folding. Chaperonins belong to a class of molecular chaperones that have been extensively studied. However, the mechanism by which a chaperonin mediates the folding of proteins is still controve...
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The original experiments reconstituting GroEL-GroES-mediated protein folding were carried out under "nonpermissive" conditions, where the chaperonin system was absolutely required and substrate proteins could not achieve the native state if diluted directly from denaturant into solution. Under "permissive" conditions, however, employing lower substrate concentration and lower temperature, some ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2008
ISSN: 0006-3495
DOI: 10.1529/biophysj.107.113209