Journal of Physical Chemistry B, Vol.109, No.49, 23175-23182, 2005
Probing structure in the polymorphic domain of the L-enantiomer of N-benzoyl-phenylalanine by means of 2D solid-state NMR spectroscopy and DFT calculations
A study of polymorphism using a range of solid-state NMR techniques is presented. We demonstrate the existence of at least six polymorphs in a sample of N-benzoyl-L-phenylalanine. We also present methodology for the characterization of the protonation state, hydrogen bonding, and molecular conformation for the polymorphs, 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 have on the chemical shift tensor.