Protein memory through altered folding mediated by intramolecular chaperones

Article Abstract:

The intramolecular chaperone of subtilisin allows folding to take place by acting as a template for its protease domain. However, it is not part of that domain. It appears that an identical polypeptide can fold into an altered conformation through a mutated intramolecular chaperone. Memory of the folding process is retained. Intramolecular chaperone-imprinted protein memory seems to be stable in aqueous environments. In contrast, enzyme memory disappears in aqueous solutions because of the conformational flexibility of enzymes.

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Chaperones classified

Article Abstract:

The division of the molecular chaperones into two classes, the hsp70 (DnaK) group and the chaperonin group, has been strengthened by new evidence that bears out earlier evidence derived from phylogenetics and cellular localization. The new evidence, which depends on the analysis of structural motifs, shows that hsp70 and the GroEL subclass of chaperonins resemble each other in having a coiled-coil domain structure. Molecular chaperones help in protein folding, protein targeting and complex assembly.

Proteins, Protein structure

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Hsp90 chaperones protein folding in vitro

Article Abstract:

Heat-shock protein 90 (Hsp90) induces protein folding by inhibiting the aggregation of non-native proteins and by attaching to the target proteins at a stoichiometry of one Hsp90 dimer to one or two substrate molecules. Hsp90 is the most common stress protein in the cytosol of eukaryotic cells. In vitro tests involving purified bovine pancreatic Hsp90 showed that Hsp90 functions as a molecular chaperone but does not require nucleoside triphosphates.

Heat shock proteins

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