Intramolecular chaperones and protein folding

Ujwal Shinde, Masayori Inouye

Research output: Contribution to journalArticle

156 Citations (Scopus)

Abstract

Many proteins from both prokaryotic and eukaryotic sources are produced with amino-terminal propeptides. These propeptides, which are usually located between the signal peptide and the mature protein, are essential for the proper function of that protein. Recent research has indicated that these polypeptides are indispensible for proper folding of the proteins they are attached to. As propeptides perform a function similar to that of a large family of heat shock proteins, they had been broadly classified as molecular chaperones. However, significant differences exist between these two classes of proteins and to distinguish them from one another, propeptides have been termed intramolecular chaperones. Recent results have suggested that such intramolecular chaperones may be found in a large number of proteins.

Original languageEnglish (US)
Pages (from-to)442-446
Number of pages5
JournalTrends in Biochemical Sciences
Volume18
Issue number11
DOIs
StatePublished - 1993
Externally publishedYes

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Protein folding
Protein Folding
Proteins
Molecular Chaperones
Protein Sorting Signals
Heat-Shock Proteins
Peptides
Research

ASJC Scopus subject areas

  • Biochemistry

Cite this

Intramolecular chaperones and protein folding. / Shinde, Ujwal; Inouye, Masayori.

In: Trends in Biochemical Sciences, Vol. 18, No. 11, 1993, p. 442-446.

Research output: Contribution to journalArticle

Shinde, Ujwal ; Inouye, Masayori. / Intramolecular chaperones and protein folding. In: Trends in Biochemical Sciences. 1993 ; Vol. 18, No. 11. pp. 442-446.
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