title: The intramolecular chaperone-mediated protein folding.
abstract: 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.
authors.affiliation: Robert Wood Johnson Medical School, Department of Biochemistry, 675 Hoes Lane, Piscataway, NJ 08854-5635, USA.
authors.forename: Yu-Jen
authors.initials: YJ
authors.lastname: Chen
authors.forename: Masayori
authors.initials: M
authors.lastname: Inouye
mesh_terms: D000818:Animals; D003461:Crystallography; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D013381:Subtilisins / Q000737:chemistry / Q000378:metabolism
chemical_list: D018832:Molecular Chaperones; D013381:Subtilisins