Force-profile analysis of the cotranslational folding of HemK and filamin domains: Comparison of biochemical and biophysical folding assays
| Autor: | Andres de la Rosa, Gunnar von Heijne, Renuka Kudva, Grant Kemp |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical Protein Folding Filamins Protein domain Filamin Ribosome Biophysical Phenomena 03 medical and health sciences 0302 clinical medicine Protein Domains Structural Biology Escherichia coli Protein Methyltransferases Molecular Biology Biological sciences 030304 developmental biology 0303 health sciences Chemistry Force profile Escherichia coli Proteins Folding (chemistry) Förster resonance energy transfer Biophysics Protein folding 030217 neurology & neurosurgery |
| DOI: | 10.1101/470831 |
| Popis: | We have characterized the cotranslational folding of two small protein domains of different folds – the a-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 - FPA), allowing us to compare FPA to three other techniques currently used to study cotranslational folding: real-time FRET, PET, 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. |
| Databáze: | OpenAIRE |
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