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À propos de : Probing Structure in the Polymorphic Domain of the l-Enantiomer ofN-Benzoyl-Phenylalanine by Means of 2D Solid-State NMR Spectroscopy and DFTCalculations        

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  • Probing Structure in the Polymorphic Domain of the l-Enantiomer ofN-Benzoyl-Phenylalanine by Means of 2D Solid-State NMR Spectroscopy and DFTCalculations
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  • A study of polymorphism using a range of solid-state NMR techniques is presented. We demonstrate theexistence of at least six polymorphs in a sample of N-benzoyl-l-phenylalanine. We also present methodologyfor the characterization of the protonation state, hydrogen bonding, and molecular conformation for thepolymorphs, together with results of such a characterization for one of the polymorphs present in our sample.DFT modeling is used to investigate the separate effects hydrogen bonding and molecular conformation haveon the chemical shift tensor.
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