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Multifunnel 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 ?-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.

SUBMITTER: Bernhardt NA 

PROVIDER: S-EPMC5823028 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Multifunnel Landscape of the Fold-Switching Protein RfaH-CTD.

Bernhardt Nathan A NA   Hansmann Ulrich H E UHE  

The journal of physical chemistry. B 20180124 5


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 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 rec  ...[more]

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