Ribosome Elongation Kinetics of Consecutively Charged Residues Are Coupled to Electrostatic Force-Reference-Cited by-同舟云学术

Ribosome Elongation Kinetics of Consecutively Charged Residues Are Coupled to Electrostatic Force

Published:2021-10-15 Issue:43 Volume:60 Page:3223-3235
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Leininger Sarah E.¹^ORCID,Rodriguez Judith²,Vu Quyen V.³^ORCID,Jiang Yang¹,Li Mai Suan³⁴^ORCID,Deutsch Carol⁵,O’Brien Edward P.¹²⁶^ORCID

Affiliation:

1. Department of Chemistry, Penn State University, University Park, Pennsylvania 16802, United States

2. Bioinformatics and Genomics Graduate Program, Huck Institutes of the Life Sciences, Penn State University, University Park, Pennsylvania 16802, United States

3. Institute of Physics, Polish Academy of Sciences, Warsaw 02-668, Poland

4. Institute for Computational Sciences and Technology, Ho Chi Minh City 700000, Vietnam

5. Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

6. Institute for Computational and Data Sciences, Penn State University, University Park, Pennsylvania 16802, United States

Funder

Division of Biological Infrastructure

Division of Molecular and Cellular Biosciences

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00507

Reference70 articles.

1. Cotranslational Protein Folding inside the Ribosome Exit Tunnel

2. Small protein domains fold inside the ribosome exit tunnel

3. Trigger Factor Reduces the Force Exerted on the Nascent Chain by a Cotranslationally Folding Protein

4. Domain topology, stability, and translation speed determine mechanical force generation on the ribosome

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