| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10822705 | Current Opinion in Structural Biology | 2005 | 6 Pages |
Abstract
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.
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Authors
Amnon Horovitz, Keith R Willison,