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  • Title: Closed state of gramicidin channel detected by X-ray in-plane scattering.
    Author: He K, Ludtke SJ, Wu Y, Huang HW, Andersen OS, Greathouse D, Koeppe RE.
    Journal: Biophys Chem; 1994 Feb; 49(1):83-9. PubMed ID: 7510532.
    Abstract:
    An analogue of gramicidin A (gA) was synthesized with the formyl group replaced by a BOC group. The analogue (BOC-gA) exhibited single channel conduction, but the channel is 5-order-of-magnitude destabilized relative to the gA channel. Hydrated mixtures of gramicidin and dilauroyl phosphatidylcholine in the molar ratio of 1:10 were prepared into uniformly aligned multiple bilayers, and X-ray scattering with the momentum transfer in the plane of the membrane was measured. Analysis with the help of computer simulations showed that 70% of BOC-gA are monomers. Thus for the first time it was shown that gramicidin monomers are stable inside the monolayers of a lipid membrane. Furthermore, the monomers have the same beta helical conformation as the dimeric channel. The result suggests the possibility that when a gramicidin channel is closed, it dissociates into two monomers floating in opposite monolayers.
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