Output details

Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer

This was a multi-institution collaboration involving the Bain group at UCL, the MRC Centre for Protein Engineering (Cambridge), Imperial College and Bar-Ilan University. The Bain group performed crucial (and extensive) fluorescence anisotropy measurements which indicated the absence of protein aggregation and also the lack of orientational restriction of the FRET fluorophores. This work underpinned the conclusion that the multiple peaks observed in the single-molecule FRET histograms arose from subpopulations of p53 protein conformers (a fundamental discovery). Previous work on protein-chaperone interactions had shown that orientational restriction and aggregation both gave rise to multiple peaks in single molecule FRET histograms.