Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5510745 | Current Opinion in Structural Biology | 2018 | 5 Pages |
Abstract
Chaperones are important in preventing protein aggregation and aiding protein folding. How chaperones aid protein folding remains a key question in understanding their mechanism. The possibility of proteins folding while bound to chaperones was reintroduced recently with the chaperone Spy, many years after the phenomenon was first reported with the chaperones GroEL and SecB. In this review, we discuss the salient features of folding while bound in the cases for which it has been observed and speculate about its biological importance and possible occurrence in other chaperones.
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Authors
Scott Horowitz, Philipp Koldewey, Frederick Stull, James CA Bardwell,