title: Chaperonins.
abstract: Molecular chaperones are essential to all living organisms. Their key role consists of mediating protein folding within the cell. Recent functional studies have provided more detailed information about the function and regulation of the chaperone network. Highlights of the past year include the crystal structure determinations of the asymmetric GroEL-GroES complex and of their isolated peptide-binding domains.
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, UK. braig@mrc-lmb.cam.ac.uk
authors.forename: K
authors.initials: K
authors.lastname: Braig
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018835:Chaperonin 10 / Q000737:chemistry; D018834:Chaperonin 60 / Q000737:chemistry; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D008954:Models, Biological; D017510:Protein Folding
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D018840:HSP70 Heat-Shock Proteins; D000255:Adenosine Triphosphate; D018833:Chaperonins