This research poster investigates changes in the structural ensemble of FoxO1, a crucial transcription factor implicated in various cellular processes. Utilizing novel carbon direct-detect NMR techniques, we analyze how the post-translational modification of acetylation influences FoxO1's conformational dynamics. Our findings shed light on the intricate interplay between FoxO1's structure and function, providing valuable insights into its regulatory mechanisms and potential therapeutic targets for diseases such as cancer and metabolic disorders.