ABSTRACT: Heat shock proteins play a significant role in response to different weather conditions. In this study, hsp70 protein sequences from cultivar c273 of Triticum aestivum were used. The main purpose for doing this research would be to execute an in-silico evaluation and estimate the 3D structure of the hsp70 protein. The aliphatic index divulge 86.33 values refers that proteins were thermal stable. The calculated grand average hydropathy value is −0.8; this value shows better interaction of the hsp70 protein with water. A thorough bioinformatics investigation of the Hsp70 gene in c273 and five different species was therefore performed in this study. A phylogenetic study separates them into six subclades. In contrast to other species, Triticum turgidum and TRINITY_DN11241_c0_g1_i4 are unique. The 3D structure of the hsp70 was done by using Swiss model. The selected model`s results were evaluated using the Saves server.  This research provide insight into Hsp70’s Recent research has elucidated the processes behind the actions of Hsp70s and their co-chaperones, indicating new possibilities for modifying disease-related Hsp70 roles.

KEYWORDS: Wheat, Protein, Secondary Structure, Triticum aestivum, Three-dimensional Structure