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Force-Profile Analysis of the Cotranslational Folding of HemK and Filamin Domains: Comparison of Biochemical and Biophysical Folding Assays
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Number of Authors: 42019 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 431, no 6, p. 1308-1314Article in journal (Refereed) Published
Abstract [en]

We have characterized the cotranslational folding of two small protein domains of different folds-the alpha-helical N-terminal domain of HemK and the beta-rich FLN5 filamin domain-by measuring the force that the folding protein exerts on the nascent chain when located in different parts of the ribosome exit tunnel (force-profile analysis, or FPA), allowing us to compare FPA to three other techniques currently used to study cotranslational folding: real-time FRET, photo induced electron transfer, and NMR. We find that FPA identifies the same cotranslational folding transitions as do the other methods, and that these techniques therefore reflect the same basic process of cotranslational folding in similar ways.

Place, publisher, year, edition, pages
2019. Vol. 431, no 6, p. 1308-1314
Keywords [en]
cotranslational folding, HemK, FLN5, arrest peptide
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-168378DOI: 10.1016/j.jmb.2019.01.043ISI: 000463120800018PubMedID: 30738895OAI: oai:DiVA.org:su-168378DiVA, id: diva2:1313657
Available from: 2019-05-06 Created: 2019-05-06 Last updated: 2019-05-06Bibliographically approved

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Kemp, GrantKudva, Renukade la Rosa, Andrésvon Heijne, Gunnar
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