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pubmed-article:9223019pubmed:abstractTextThe terminally blocked tetrapeptide pBrBz-[D-(alpha Me)Leu]2-D-(alpha Me)Val-D-(alpha Me)Leu-OfBu is folded in the crystal state in a left-handed 3(10)-helical structure stabilized by two consecutive 1<--4 C = O...H-N intramolecular H-bonds, as determined by X-ray diffraction analysis. A CD study strongly supports the view that this conformation is also that largely prevailing in MeOH solution. A comparison with the published conformation of pBrBz-[D-(alpha Me)Leu]4-OfBu indicates that incorporation of a single internal beta-branched (alpha Me)Val guest residue into the host homo-tetrapeptide from the gamma-branched (alpha Me)Leu residue is responsible for a dramatic structural perturbation, i.e. an inversion of the 3(10) screw sense from right to left-handed.lld:pubmed
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pubmed-article:9223019pubmed:pagination396-402lld:pubmed
pubmed-article:9223019pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9223019pubmed:articleTitleInversion of 3(10)-helix screw sense in a (D-alpha Me)Leu homo-tetrapeptide induced by a guest D-(alpha Me)Val residue.lld:pubmed
pubmed-article:9223019pubmed:affiliationDepartment of Organic Chemistry, University of Padova, Italy.lld:pubmed
pubmed-article:9223019pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9223019pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed