The intramolecular chaperone-mediated protein folding

Yu Jen Chen, Masayori Inouye

Research output: Contribution to journalReview articlepeer-review

79 Scopus citations


Some proteins have evolved to contain a specific sequence as an intramolecular chaperone, which is essential for protein folding but not required for protein function, as it is removed after the protein is folded by autoprocessing or by an exogenous protease. To date, a large number of sequences encoded as N-terminal or C-terminal extensions have been identified to function as intramolecular chaperones. An increasing amount of evidence has revealed that these intramolecular chaperones play an important role in protein folding both in vivo and in vitro. Here, we summarize recent studies on intramolecular chaperone-assisted protein folding and discuss the mechanisms as to how intramolecular chaperones play roles in protein folding.

Original languageEnglish (US)
Pages (from-to)765-770
Number of pages6
JournalCurrent Opinion in Structural Biology
Issue number6
StatePublished - Dec 2008

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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