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.
Researcher Thomas found that HMGB1 plays a supporting role in the binding of transcription factors like p53 to DNA. In 2012, her team used NMR spectroscopy again to determine the structure of the A-box/p53 complex resulting from the interaction between p53's N-terminus and one HMG-box of HMGB1.