Sixteen and 24 membered aza-beta(3)-peptidic macrocycles containing a alpha-hydrazinoacid or a beta(3)-aminoacid were synthesized. The conformation of these pseudopeptides was determined by using NH chemical shift analysis, NH extinction, VT-NMR experiments, and X-ray diffraction. The study shows that a stable conformation is retained between 223 and 413 K. The latter is characterized by an uninterrupted internal H-bond network and a syndiotactic arrangement of the asymmetric centers. It means that the presence of the optically pure residue acts as a conformational lock to select a single enantiomer through the cyclization by controlling the absolute configuration of all the nitrogen atoms. To our knowledge, this represents the first example of a dynamic enantioselection process involving several centers prone to pyramidal inversion. These results give a new impulsion to the control of nitrogen chirality, which remained limited to small cycles for 60 years.