bioRxiv · 10.1101/221143
Multi-Funnel Landscape of the Fold-Switching Protein RfaH-CTD
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 {beta}-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.\n\n\n\nO_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=109 SRC=\"FIGDIR/small/221143_ufig1.gif\" ALT=\"Figure 1\">\nView larger version (23K):\norg.highwire.dtl.DTLVardef@17ce490org.highwire.dtl.DTLVardef@81ce9aorg.highwire.dtl.DTLVardef@230ddborg.highwire.dtl.DTLVardef@162be94_HPS_FORMAT_FIGEXP M_FIG TOC Image\n\nC_FIG
Source connections
Explore related subjects
Keep this discovery
Bernhardt, N. A., Hansmann, U.. 2017-11-17. Multi-Funnel Landscape of the Fold-Switching Protein RfaH-CTD. https://doi.org/10.1101/221143
Cite the original work for its findings. Save a collection to share your selection of sources.