The driving force for co-translational protein folding is weaker in the ribosome vestibule due to greater water ordering-Reference-Cited by-同舟云学术

The driving force for co-translational protein folding is weaker in the ribosome vestibule due to greater water ordering

Published:2021 Issue:35 Volume:12 Page:11851-11857
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Vu Quyen V.¹^ORCID,Jiang Yang²^ORCID,Li Mai Suan¹³^ORCID,O'Brien Edward P.²⁴⁵

Affiliation:

1. Institute of Physics, Polish Academy of Sciences, Al. Lotnikow 32/46, 02-668 Warsaw, Poland

2. Department of Chemistry, Penn State University, University Park, Pennsylvania, USA

3. Institute for Computational Sciences and Technology, Quang Trung Software City, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City, Vietnam

4. Bioinformatics and Genomics Graduate Program, The Huck Institutes of the Life Sciences, Penn State University, University Park, Pennsylvania, USA

5. Institute for Computational and Data Sciences, Penn State University, University Park, Pennsylvania, USA

Abstract

In the ribosome vestibule, the contact minimum between two methane molecules is half as stable as compared to in bulk solution, demonstrating that the hydrophobic effect is weakened in the vestibule of ribosome exit tunnel.

Funder

National Institutes of Health

National Science Foundation

Narodowe Centrum Nauki

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D1SC01008E

Reference40 articles.

1. Dominant forces in protein folding

2. Computational and Theoretical Methods for Protein Folding

3. Transient Tertiary Structure Formation within the Ribosome Exit Port

4. New Scenarios of Protein Folding Can Occur on the Ribosome

5. Cotranslational Protein Folding inside the Ribosome Exit Tunnel

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1. Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding;Journal of Chemical Information and Modeling;2024-08-16

2. The ribosome lowers the entropic penalty of protein folding;Nature;2024-08-07

3. The critical role of co-translational folding: An evolutionary and biophysical perspective;Current Opinion in Systems Biology;2024-03

4. Simulation of Complex Biomolecular Systems: The Ribosome Challenge;Annual Review of Biophysics;2023-05-09

5. The protein escape process at the ribosomal exit tunnel has conserved mechanisms across the domains of life;The Journal of Chemical Physics;2023-01-07