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pubmed-article:1382580pubmed:abstractTextA conformational transition is described for the polypeptide, gramicidin A, in which a dimer that forms a left-handed intertwined antiparallel helix is converted to a single-stranded amino terminus to amino terminus right-handed helix. The starting structure is determined here by solution NMR methods while reference is made to the well-established folding motif of gramicidin in a lipid bilayer for the ultimate conformation of this transition. Furthermore, an organic solvent system of benzene and ethanol in which gramicidin has a unique conformation is identified. This conformation is shown to be very similar to that derived from X-ray diffraction of crystals prepared from a similar solvent system.lld:pubmed
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pubmed-article:1382580pubmed:articleTitleA conformational rearrangement in gramicidin A: from a double-stranded left-handed to a single-stranded right-handed helix.lld:pubmed
pubmed-article:1382580pubmed:affiliationDepartment of Chemistry, Florida State University, Tallahassee 32306-3006.lld:pubmed
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pubmed-article:1382580pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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