This study combined protein modeling methods to generate the prolamins' fractions as precise as possible. Hence, gliadins, zeins, kafirins, hordeins, secalins, avenins and oryzins were generated based on their characteristics and disulfide mapping. Findings were briefly as follows: (i) Gliadins and hordeins were homologous to have both globular and rod-like structures. The omega-gliadin and C-hordein showed their worm-like structures. (ii) Zeins and kafirins had homology and existed in ordered helical-rich models. (iii) The gamma-secalins exhibited similar models to that of gamma-gliadin, indicating a ring connected to a tail. (iv) Avenins and Oryzins formed all possible disulfide bonds, however, there was an unusual linkage between two tandem cysteines of avenins. The studies on 3D structure of prolamins are hopefully expected to provide an improved insight at molecular level leading to accurate functionalization and applications of them in various field of studies including biology, food and medicine.