Protein folding in the cell

Nature. 1992 Jan 2;355(6355):33-45. doi: 10.1038/355033a0.


In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the absence of other macromolecular cellular components, folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.

Publication types

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

MeSH terms

  • Amino Acid Isomerases / metabolism
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / metabolism
  • Cell Physiological Phenomena*
  • Heat-Shock Proteins / metabolism
  • Isomerases / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Peptidylprolyl Isomerase
  • Protein Conformation*
  • Protein Disulfide-Isomerases
  • Proteins / metabolism*
  • Thioredoxins / metabolism


  • Carrier Proteins
  • Heat-Shock Proteins
  • Proteins
  • Thioredoxins
  • Isomerases
  • Amino Acid Isomerases
  • Peptidylprolyl Isomerase
  • Protein Disulfide-Isomerases