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The longest, regular polypeptide 3(10) helix at atomic resolution.

V Pavone·B Di Blasio·A Santini·E Benedetti·C Pedone·C Toniolo·M Crisma
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Abstract

A synthetic, terminally blocked homodecapeptide from the C alpha, alpha-dimethylated glycyl residue alpha-aminoisobutyric acid has been analyzed by single-crystal X-ray diffraction and the structure refined to R = 0.073. The compound crystallizes as a perfect 3(10) helix, stabilized by eight consecutive intramolecular N-H . . . O = C hydrogen bonds. This is the first observation at atomic resolution of a regular polypeptide 3(10) helix as long as three complete turns.

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Aminoisobutyric AcidsChemical PhenomenaChemistry, PhysicalHydrogen BondingMolecular StructureOligopeptidesProtein ConformationX-Ray DiffractionJournal Article

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V Pavone, B Di Blasio, A Santini, E Benedetti, C Pedone, C Toniolo, M Crisma. 1990-08-05. The longest, regular polypeptide 3(10) helix at atomic resolution.. https://doi.org/10.1016/0022-2836(90)90279-u

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