Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 431, Issue 6, Pages 1308-1314Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.01.043
Keywords
cotranslational folding; HemK; FLN5; arrest peptide
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Funding
- Knut and Alice Wallenberg Foundation [2012.0282]
- Swedish Cancer Foundation [15 0888]
- Swedish Research Council [621-2014-3713]
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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. (C) 2019 Elsevier Ltd. All rights reserved.
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