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Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.

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Resource Type: Journal article/Issue, Review, Diagram, Graph/chart
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Continuing education

Author and Copyright


Authors and Editors: Sue Wickner of Laboratory of Molecular Biology, National Cancer Institute, Michael Maurizi of Laboratory of Cell Biology, National Cancer Institute, Susan Gottesman of Laboratory of Molecular Biology, National Cancer Institute
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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American Association for the Advancement of Science


     
   

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