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
15m
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))

Speaker

Mr Adekunle Aina (Memorial University of Newfoundland)

Description

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)

Co-author

Stefan Wallin (Memorial University of Newfoundland)

Presentation Materials