An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel
Guzman-Luna et al. present a crosslinking analysis of the interaction of unstructured nascent chains with ribosomal proteins near the nascent polypeptide exit tunnel of the ribosome. They further analyze the dependence of these interactions on the peptide length, surface charge and ionic strength (i...
Main Authors: | Valeria Guzman-Luna, Andrew M. Fuchs, Anna J. Allen, Alexios Staikos, Silvia Cavagnero |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2021-10-01
|
Series: | Communications Biology |
Online Access: | https://doi.org/10.1038/s42003-021-02752-4 |
Similar Items
-
Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel
by: Daniel M. Wilson, et al.
Published: (2020-10-01) -
The ribosome modulates folding inside the ribosomal exit tunnel
by: Florian Wruck, et al.
Published: (2021-05-01) -
Cotranslational Protein Folding inside the Ribosome Exit Tunnel
by: Ola B. Nilsson, et al.
Published: (2015-09-01) -
Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
by: Linda Schulte, et al.
Published: (2020-11-01) -
Non-bulk-like solvent behavior in the ribosome exit tunnel.
by: Del Lucent, et al.
Published: (2010-10-01)