title: Principles of chaperone-mediated protein folding.
abstract: The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.
authors.affiliation: Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
authors.forename: F U
authors.initials: FU
authors.lastname: Hartl
mesh_terms: D018834:Chaperonin 60 / Q000737:chemistry*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D018834:Chaperonin 60; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones