We have examined the preferred 3D structure of homopeptides based on an alpha-amino acid lacking the asymmetry at the alpha-carbon but exhibiting chirality in the side chains (at the two beta-carbons). These joint stereochemical properties are remarkably unusual for an alpha-amino acid. To this end, we carried out an experimental investigation by X-ray diffraction and NMR spectrometry. The results point to a well-defined relationship between screw sense of the turn and helix structures formed and side-chain configurations.
Turn and Helical Peptide Handedness Governed Exclusively by Side-Chain Chiral Centers
Fernando Formaggio;Marco Crisma;Claudio Toniolo
2005
Abstract
We have examined the preferred 3D structure of homopeptides based on an alpha-amino acid lacking the asymmetry at the alpha-carbon but exhibiting chirality in the side chains (at the two beta-carbons). These joint stereochemical properties are remarkably unusual for an alpha-amino acid. To this end, we carried out an experimental investigation by X-ray diffraction and NMR spectrometry. The results point to a well-defined relationship between screw sense of the turn and helix structures formed and side-chain configurations.File in questo prodotto:
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