Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study-Reference-Cited by-同舟云学术

Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study

Published:2023-05-18 Issue:21 Volume:127 Page:4761-4774
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Vu Quyen V.¹^ORCID,Nissley Daniel A.²^ORCID,Jiang Yang³^ORCID,O’Brien Edward P.³⁴⁵^ORCID,Li Mai Suan¹⁶^ORCID

Affiliation:

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

2. Department of Statistics, University of Oxford, Oxford OX1 3LB, U.K.

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

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

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

6. Institute for Computational Sciences and Technology, Quang Trung Software City, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City 700000, Vietnam

Funder

Division of Molecular and Cellular Biosciences

Narodowe Centrum Nauki

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.3c01694

Reference55 articles.

1. The Geometry of the Ribosomal Polypeptide Exit Tunnel

2. Structural Origins of FRET-Observed Nascent Chain Compaction on the Ribosome

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

4. Small protein domains fold inside the ribosome exit tunnel

5. Cotranslational Protein Folding inside the Ribosome Exit Tunnel

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