Protein folding in the cell: molecular chaperones pave the way.
In vitro, many unfolded polypeptides are able to fold to the native state spontaneously, indicating that the amino acid sequence of a protein contains all the information necessary to specify its three-dimensional conformation. It had been assumed that protein folding in vivo also generally occurs in a spontaneous process. This view has changed only recently due to the discovery of a number of proteins, now commonly called 'molecular chaperones', which are essential for cellular protein folding and occur ubiquitously in eubacteria, archaebacteria and in eukaryotic cells.
Martin
J
J
Cellular Biochemisty and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
Hartl
F U
FU
D000255:Adenosine Triphosphate / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate; C063842:dnaK protein, E coli