University of Tehran Journal of Sciences, Islamic Republic of Iran 1016-1104 9 2 1998 06 01 MOLECULAR MODELING AND NMR STUDY OF HISTDINIE AND ITS ANALOGUES AS , PYRIDOXAL 5 '-PHOSPHATE DEPENDENT HISTIDINE DECARBOXYLASE INHIBITORS - 31464 EN Journal Article Molecular modeling analysis of charge density and heat of fornation by PM3 method as well as C, H NMR and 2D-NMR measurements of histidine (substrate) and some of its derivatives as histidine decarboxylase inhibitors were performed. It was established that the atom, usually nitrogen, which forms internal aldimine with pyridoxal5 -phosphate (PLP), (coenzyme), has negative and almost equal charge in histidine and ather inhibittors. The preferred ccznfom&on of compounds with higher inhibitory activity is calculated to be in such a form that the amino group and imidazole ring have a dihedral angle of 60?. In this conformation, molecules are able to form internal hydrogen bonds. In contrast, their derivatives with lower activity have adifferent conformation. NMR measurements support our theoretical calculations https://jsciences.ut.ac.ir/article_31464_49030e99dc6676fa7a0ae152ce0c68c7.pdf