Molecular chaperones. Opening and closing the Anfinsen cage.
Dynamic interactions between chaperonins allow newly synthesized polypeptides to begin correct folding inside a transiently closed cage. Specialized chaperonins may be used to deal with recalcitrant proteins.
Ellis
R J
RJ
Department of Biological Sciences, University of Warwick, UK.
D000255:Adenosine Triphosphate / Q000502:physiology; D018835:Chaperonin 10 / Q000737:chemistry / Q000502:physiology; D018834:Chaperonin 60 / Q000737:chemistry / Q000502:physiology; D018833:Chaperonins / Q000502:physiology*; D046911:Macromolecular Substances; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D014764:Viral Proteins / Q000502:physiology
D018835:Chaperonin 10; D018834:Chaperonin 60; D046911:Macromolecular Substances; D014764:Viral Proteins; C063473:gene 31 protein, Enterobacteria phage T4; D000255:Adenosine Triphosphate; D018833:Chaperonins