10-16 June 2018
Dalhousie University
America/Halifax timezone
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Escherichia coli's RfaH studied by all-atom Monte Carlo simulation (G)*

13 Jun 2018, 14:00
SUB 302 (cap. 40) (Dalhousie University)

SUB 302 (cap. 40)

Dalhousie University

Oral Competition (Graduate Student) / Compétition orale (Étudiant(e) du 2e ou 3e cycle) Physics in Medicine and Biology / Physique en médecine et en biologie (DPMB-DPMB) W3-4 Soft matter and molecular dynamic (DPMB/DCMMP) | Matière molle et dynamique moléculaire (DPMB/DPMCM))


Mr Adekunle Aina (Memorial University of Newfoundland)


RfaH is a compact two-domain multi-functional protein from the bacteria $Escherichia\ coli\ (E. coli)$. Its C-terminal domain (CTD) has been shown experimentally to be able to undergo a complete conformational change from an $\alpha$-helix bundle to a $\beta$-barrel structure. The $\alpha$-helix bundle to $\beta$-barrel fold switch accounts for the observed dual role of RfaH, whereby it regulates transcription as well as enhances translation. We employ all-atom Monte Carlo simulations to investigate the stabilities of the two structural forms of RfaH and the character of transition between them. Our simulations reveal that the stand-alone $\alpha$-helix CTD is relatively unstable despite the stabilizing interactions with the N-terminal domain (NTD). Moreover, we observe the stability of the stand-alone $\beta$-barrel conformation to be always higher than the $\alpha$-helix bundle structure. Thus, we conclude that the $\alpha$-helix bundle to $\beta$-barrel fold switch of the CTD in RfaH is thermodynamically favoured in our model.

Primary author

Mr Adekunle Aina (Memorial University of Newfoundland)


Stefan Wallin (Memorial University of Newfoundland)

Presentation Materials