Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone

<p>Trigger factor (TF) is a highly conserved multi-domain molecular chaperone that exerts its chaperone activity at the ribosomal tunnel exit from which newly synthesized nascent chains emerge. TF also displays promiscuous substrate binding for a large number of cytosolic proteins independent...

Full description

Bibliographic Details
Main Authors: C.-T. Huang, Y.-C. Lai, S.-Y. Chen, M.-R. Ho, Y.-W. Chiang, S.-T. D. Hsu
Format: Article
Language:English
Published: Copernicus Publications 2021-06-01
Series:Magnetic Resonance
Online Access:https://mr.copernicus.org/articles/2/375/2021/mr-2-375-2021.pdf