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Conformational restrictions of peptides via backbone modification: Solution and crystal-state analysis of Boc-L-Pro-DZPhe-Gly-NH2
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1991
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Peptide EngineeringMolecular BiologyConformational RestrictionsOrganic ChemistryChemistryN-alpha-protected ModelProtein FoldingType Ii-iiiStructure ElucidationProtein ChemistryBiochemistryBackbone ModificationCrystal-state AnalysisConformational StudyCrystal StateCrystallographyCrystal Structure DesignStructural BiologyNatural SciencesPeptide LibraryPeptide SynthesisProtein EngineeringMedicine
An N-alpha-protected model tripeptide amide containing, in the central position, an alpha,beta-dehydrophenylalanine (Z-configurational isomer), Boc-L-Pro-DELTA-Z-Phe-Gly-NH2 (Boc, tert-butyloxycarbonyl), has been synthesized by solution methods and fully characterized. IR absorption and H-1 NMR studies provided evidence for the occurrence of a significant population of a conformer containing two consecutive, intramolecularly H-bonded (type II-III') beta-bends in solution. However, an X-ray diffraction analysis clearly indicates that only the type-II beta-bend structure survives in the crystal state.