Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 122, Issue 5, Pages 1600-1607Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b11352
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Funding
- National Science Foundation [MCB160005, CHE1266256]
- National Institute of Health [GM120578, GM120634]
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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 C-terminal domain, dubbed by us as RfaH-C-terminal domain (RfaH-CTD), and is studied here with a variant of the replica exchange-with-tunneling 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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