Molecular chaperones: avoiding the crowd.
The involvement of two types of molecular chaperone in folding newly synthesized proteins can be rationalized in terms of the crowded nature of the intracellular environment. Recent work sheds light on how these chaperones recognise their substrates and protect them from the problems of macromolecular crowding.
Ellis
R J
RJ
Department of Biological Sciences, University of Warwick Coventry, CV4 7AL, UK. je@dna.bio.warwick.ac.uk
D000818:Animals; D001665:Binding Sites; D018834:Chaperonin 60 / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
D018834:Chaperonin 60; D018832:Molecular Chaperones