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.
Hughes
Colan E
CE
Department for NMR-Based Structural Biology, Max-Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. hughesce@cardiff.ac.uk
Olejniczak
Sebastian
S
Helinski
Jan
J
Ciesielski
Włodzimierz
W
Repisky
Michal
M
Andronesi
Ovidiu C
OC
Potrzebowski
Marek J
MJ
Baldus
Marc
M
D003198:Computer Simulation; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008956:Models, Chemical; D008968:Molecular Conformation; D015335:Molecular Probes / Q000737:chemistry*; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry; D019920:Photoaffinity Labels / Q000737:chemistry*; D011789:Quantum Theory; D013237:Stereoisomerism
D015335:Molecular Probes; D019920:Photoaffinity Labels; D010649:Phenylalanine; C053764:benzoylphenylalanine