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