Resolving the 3D spatial orientation of helix I in the closed state of the colicin E1 channel domain by FRET. Insights into the integration mechanism

Current evidence suggests that the closed-state membrane model for the channel-forming domain of colicin E1 involves eight amphipathic α-helices (helices I–VII and X) that adopt a two-dimensional arrangement on the membrane surface. Two central hydrophobic α-helices in colicin E1 (VIII and IX) adopt...

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Veröffentlicht in:Archives of biochemistry and biophysics 2016-10, Vol.608, p.52-73
Hauptverfasser: Lugo, Miguel R., Ho, Derek, Merrill, A. Rod
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Sprache:eng
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