Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 2, issue 1
Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-375-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-375-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Articles | Volume 2, issue 1
Research article
 | 
04 Jun 2021
Research article |  | 04 Jun 2021

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

Chih-Ting Huang, Yei-Chen Lai, Szu-Yun Chen, Meng-Ru Ho, Yun-Wei Chiang, and Shang-Te Danny Hsu

Viewed

Total article views: 2,229 (including HTML, PDF, and XML)
HTML PDF XML Total Supplement BibTeX EndNote
1,323 805 101 2,229 279 75 63
  • HTML: 1,323
  • PDF: 805
  • XML: 101
  • Total: 2,229
  • Supplement: 279
  • BibTeX: 75
  • EndNote: 63
Views and downloads (calculated since 25 Jan 2021)
Cumulative views and downloads (calculated since 25 Jan 2021)

Viewed (geographical distribution)

Total article views: 2,229 (including HTML, PDF, and XML) Thereof 2,052 with geography defined and 177 with unknown origin.
Country # Views %
  • 1
1
 
 
 
 
Latest update: 14 May 2025
Download
Short summary
Trigger factor (TF) is a conserved bacterial molecular chaperone that exists in a monomer–dimer equilibrium in solution. It binds to the ribosome as a monomer to facilitate folding of nascent polypeptide chains. We showed that dimeric TF exhibits distinct domain dynamics and conformational polymorphism and that TF contains multiple substrate binding sites that are only accessible in its monomeric form. The equilibrium of TF in different oligomeric states may serve as a regulatory mechanism.
Read more
Share
Special issue
Robert Kaptein Festschrift