This work focuses on the biophysical characterization of protein AHA1, using techniques such as circular dichroism, intrinsic fluorescence of tryptophan and SEC-MALS; other experiments will be performed in the future. By studying these characteristics of AHA1, we aim to better understand its structure, how the complex with Hsp90 is formed, and elucidate possible functional mechanisms related to Hsp90. The AHA1 protein studied in this work comes from Sorghum bicolor.