 Alpha-fold has been successful in predicting the 3D structures of proteins from their amino acid sequences, but it's accuracy in predicting the effects of single mutations on protein stability and function remains unclear. In this study, we examined the correlation between alpha-fold's output metrics and the changes in protein stability and fluorescence, caused by single mutations. We found that there was little to no correlation between these two sets of data, suggesting that alpha-fold may not be applicable to all problems related to protein folding. This article was authored by Marina A. Pack, Karina A. Markiva, Maria S. Navacova, and others.