Waudby, Christopher A. and Dobson, C.M. and Christodoulou, John (2019) Nature and regulation of protein folding on the ribosome. Trends in Biochemical Sciences , ISSN 0968-0004.
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Abstract
Co-translational protein folding is an essential process by which cells ensure the safe and efficient production and assembly of new proteins in their functional native states following biosynthesis on the ribosome. In this review, we describe recent progress in probing the changes during protein synthesis of the free energy landscapes that underlie co-translational folding and discuss the critical coupling between these landscapes and the rate of translation that ultimately determines the success or otherwise of the folding process. Recent developments have revealed a variety of mechanisms by which both folding and translation can be modulated or regulated, and we discuss how these effects are utilised by the cell to optimise the outcome of protein biosynthesis. [Abstract copyright: Copyright © 2019 The Authors. Published by Elsevier Ltd.. All rights reserved.]
Metadata
Item Type: | Article |
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Keyword(s) / Subject(s): | co-translational folding, free energy landscape, molecular chaperones, protein synthesis, translation kinetics |
School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
SWORD Depositor: | Mr Joe Tenant |
Depositing User: | Mr Joe Tenant |
Date Deposited: | 18 Sep 2019 09:08 |
Last Modified: | 02 Aug 2023 17:52 |
URI: | https://eprints.bbk.ac.uk/id/eprint/28296 |
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