 She later described the structure of these interactions as collapsed and sandwich-like, suggesting that it is important for the dynamic activity of the DNA-binding proteins.Thomas also found that HMGB1 plays a role as a chaperone in the binding of transcription factors like p53 to DNA.In 2012, again using NMR spectroscopy, her team solved the structure of the A-box/p53 complex formed by the interaction between the N-terminus of p53 and a single HMG-box of HMGB1.