The study looked at how heat affects wheat gluten proteins, focusing on their structure and properties. Gliadin, a type of gluten protein, is resistant to heat and slows down the cooking process. Heating changes the structure of the proteins, reducing their fluorescence. High temperatures decrease certain chemical groups in gluten and glutenin, but not in gliadin. Gliadin's disulphide bonds remain stable. As the temperature increases, all protein fractions become more compact. Gliadin is more stable than glutenin, making it harder for gluten to form a network. These findings can help improve how we cook, process, and store gluten proteins.