Approaches to the isolation and characterization of molecular chaperones

Protein Expr Purif. 2006 Mar;46(1):1-15. doi: 10.1016/j.pep.2005.08.005. Epub 2005 Sep 8.

Abstract

Molecular chaperones are integral components of the cellular machinery involved in ensuring correct protein folding and the continued maintenance of protein structure. An understanding of these ubiquitous molecules is key to finding cures to protein misfolding diseases such as Alzheimer's and Creutzfeldt-Jacob diseases. In addition, further understanding of chaperones will enhance our comprehension of the way the body copes with the environmental stresses that humans encounter daily. Our laboratory and our collaborators specialize in the production and characterization of chaperones from a wide variety of sources in order to gain a fuller understanding of how chaperones function in the cell. In this review, we primarily use the Hsp70/Hsp40 chaperone pair as an example to discuss recent advances in technology and reductions in cost that lend themselves to chaperone purification from both native and recombinant sources. Common assays to assess purified chaperone activity are also discussed.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Alzheimer Disease / metabolism
  • Creutzfeldt-Jakob Syndrome / metabolism
  • Endoplasmic Reticulum / metabolism
  • Enzymes / chemistry
  • Enzymes / isolation & purification
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism
  • Humans
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / isolation & purification*
  • Molecular Chaperones / metabolism
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins / metabolism

Substances

  • Enzymes
  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones
  • Recombinant Proteins
  • Adenosine Triphosphatases