Reshaping of the conformational search of a protein by the chaperone trigger factor

The bacterial chaperone named trigger factor is found to stabilize protein folding intermediates that eventually convert to the native state, suggesting that chaperones play a direct role in instructing protein folding.

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Bibliographic Details
Main Authors:	Mashaghi Tabari, Alireza (Author) , Kramer, Günter (Author) , Bechtluft, Philipp (Author) , Zachmann-Brand, Beate (Author) , Driessen, Arnold J. M. (Author) , Bukau, Bernd (Author) , Tans, Sander J. (Author)
Format:	Article (Journal) Editorial
Language:	English
Published:	7 July 2013
In:	Nature Year: 2013, Volume: 500, Pages: 98-101
ISSN:	1476-4687
DOI:	10.1038/nature12293
Online Access:	Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nature12293 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nature12293
Author Notes:	Alireza Mashaghi, Günter Kramer, Philipp Bechtluft, Beate Zachmann-Brand, Arnold J.M. Driessen, Bernd Bukau & Sander J. Tans

Description
Summary:	The bacterial chaperone named trigger factor is found to stabilize protein folding intermediates that eventually convert to the native state, suggesting that chaperones play a direct role in instructing protein folding.
Item Description:	Gesehen am 25.06.2021
Physical Description:	Online Resource
ISSN:	1476-4687
DOI:	10.1038/nature12293