The integration of computational protein structure predictions from AlphaFold and RoseTTAFold into experimental repositories signifies a paradigm shift in structural biology where *in silico* models are treated with the same accessibility standards as experimentally determined structures (e.g., X-ray crystallography, NMR). This concept relies on the theoretical framework that high-confidence predicted coordinates can functionally substitute for missing experimental data when specific statistical confidence metrics fall within defined reliability thresholds. Consequently, this expands the domain of structural proteomics to include a comprehensive dataset encompassing both empirical and algorithmically generated conformations without requiring primary sequence re-simulation by users.
The integration of computational protein structure predictions from AlphaFold and RoseTTAFold into experimental repositories signifies a paradigm shift in structural biology where *in silico* models …