Allosteric regulation of chaperonins.
Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling between allosteric transitions and protein folding reactions. However, various mechanistic issues remain to be resolved.
Horovitz
Amnon
A
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. amnon.horovitz@weizmann.ac.il
Willison
Keith R
KR
D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D018834:Chaperonin 60 / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics
D018834:Chaperonin 60; D000255:Adenosine Triphosphate; D018833:Chaperonins