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Multi-Funnel Landscape of the Fold-Switching Protein RfaH-CTD

Nathan A. Bernhardt, Ulrich H.E. Hansmann
doi: https://doi.org/10.1101/221143
Nathan A. Bernhardt
Dept. of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019, USA
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Ulrich H.E. Hansmann
Dept. of Chemistry & Biochemistry, University of Oklahoma, Norman, OK 73019, USA
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Abstract

Proteins such as the transcription factor RfaH can change biological function by switching between distinct three-dimensional folds. RfaH regulates transcription if the C-terminal domain folds into a double helix bundle, and promotes translation when this domain assumes a β-barrel form. This fold-switch has been also observed for the isolated domain, dubbed by us RfaH-CTD, and is studied here with a variant of the RET approach recently introduced by us. We use the enhanced sampling properties of this technique to map the free energy landscape of RfaH-CTD and to propose a mechanism for the conversion process.

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Posted November 17, 2017.
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Multi-Funnel Landscape of the Fold-Switching Protein RfaH-CTD
Nathan A. Bernhardt, Ulrich H.E. Hansmann
bioRxiv 221143; doi: https://doi.org/10.1101/221143
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Multi-Funnel Landscape of the Fold-Switching Protein RfaH-CTD
Nathan A. Bernhardt, Ulrich H.E. Hansmann
bioRxiv 221143; doi: https://doi.org/10.1101/221143

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