Force-Profile Analysis of the Cotranslational Folding of HemK and Filamin Domains: Comparison of Biochemical and Biophysical Folding Assays |
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| Institution: | 1. Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden;2. Science for Life Laboratory, Stockholm University, Box 1031, SE-171 21 Solna, Sweden;1. Science for Life Laboratory and Department of Biochemistry and biophysics, Stockholm University, Tomtebodav 23, 171 21 Solna, Sweden;2. Centre of New Technologies, University of Warsaw, Banacha 2c, 02097 Warsaw, Poland;1. Department of Chemistry and Biochemistry, and Center for One Health Studies, Berry College, Mt. Berry, GA 30149, USA;2. Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retrovirus Research, Ohio State University, Columbus, OH 43210, USA;1. Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA;2. Department of Biological Sciences, Texas Tech University, Lubbock, TX 79409, USA;3. Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden;4. Sweden and Science for Life Laboratory Stockholm University, SE-171 21 Solna, Sweden;1. Molecular Medicine Program, The Hospital for Sick Children Research Institute, Toronto M5G 0A4, Ontario, Canada;2. Department of Biochemistry, University of Toronto, Toronto M5S 1A8, Ontario, Canada;3. Department of Biochemistry & Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden;1. Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden;2. Science for Life Laboratory, Stockholm University, SE-17177 Solna, Sweden |
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| Abstract: | We have characterized the cotranslational folding of two small protein domains of different folds—the α-helical N-terminal domain of HemK and the β-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, photoinduced 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. |
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