Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

Trends Biochem Sci. 1994 May;19(5):205-11. doi: 10.1016/0968-0004(94)90023-x.


Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Chaperonins
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / physiology*
  • Molecular Sequence Data
  • Protein Folding*
  • Proteins / physiology*


  • Heat-Shock Proteins
  • Proteins
  • Chaperonins