Folding while Bound to Chaperones

Authors

Scott Horowitz, University of DenverFollow
Philipp Koldewey, University of Michigan
Frederick Stull, University of Michigan
James CA Bardwell, University of Michigan

Publication Date

7-19-2017

Document Type

Article

Organizational Units

Chemistry and Biochemistry, Knoebel Institute for Healthy Aging

Keywords

Chaperones, Protein aggregation, Protein folding

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.

Publication Statement

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Recommended Citation

Horowitz, Scott, Koldewey, Philipp, Stull, Frederick, & Bardwell, James CA. (2018). Folding while bound to chaperones. Current Opinion in Structural Biology, 48, 1-5. doi: 10.1016/j.sbi.2017.06.009.