 The new computational tool, Alpha Fold 2, has been used to accurately predict the three-dimensional structure of glucose transporter, GLUT, proteins with 12 transmembrane helical segments. These proteins are essential for cellular energy supply, cell metabolism, and other vital biological processes. Additionally, they have been implicated in cancer proliferation and metastasis, making them an important target in combating cancer. However, membrane transporters are difficult to study due to their multi-spanning transmembrane properties. To overcome this challenge, researchers have developed a systematic approach called the quantity code, which replaces hydrophobic amino acids with more hydrophilic amino acids, such as glutamine, threnine, and tyrosine. This process renders the protein water soluble and allows it to be studied using traditional methods. Researchers have applied this technique to several membrane proteins, including gluts, and found that the resulting water soluble variants closely resemble the original protein structure. In this study, researchers compared the native structure of gluts with their water soluble Q. This article was authored by Eva Smorodina, Fei Dao, Rui Qing, and others.