The structural and functional organization of intramolecular chaperones

The N-terminal propeptides which mediate protein folding

Ujwal Shinde, Masayori Inouye

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

A large number of prokaryotic as well as eukaryotic proteins are produced with amino terminal propeptides. These amino-terminal extensions are essential for mediating proper folding of their corresponding proteins and are also termed as intramolecular chaperones. Though these propeptides are highly specific and unique in their function, several common features have been identified and indicate that the overall mechanism by which they function may be very similar.

Original languageEnglish (US)
Pages (from-to)629-636
Number of pages8
JournalJournal of Biochemistry
Volume115
Issue number4
StatePublished - Apr 1994
Externally publishedYes

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Protein folding
Protein Folding
Proteins
Protein
Folding
Common features

Keywords

  • Intramolecular chaperone
  • Propeptides
  • Protein folding
  • Subtilisin

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

The structural and functional organization of intramolecular chaperones : The N-terminal propeptides which mediate protein folding. / Shinde, Ujwal; Inouye, Masayori.

In: Journal of Biochemistry, Vol. 115, No. 4, 04.1994, p. 629-636.

Research output: Contribution to journalArticle

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